Page last updated: 2024-08-17

acrylamide and tryptophan

acrylamide has been researched along with tryptophan in 246 studies

Research

Studies (246)

TimeframeStudies, this research(%)All Research%
pre-199033 (13.41)18.7374
1990's82 (33.33)18.2507
2000's100 (40.65)29.6817
2010's30 (12.20)24.3611
2020's1 (0.41)2.80

Authors

AuthorsStudies
Martorana, GE; Meucci, E; Miggiano, GA; Mordente, A; Santini, SA1
Horowitz, PM; Lee, JC; Yeh, LC1
Gonzalez, L; Maegley, KA; Reich, NO; Smith, DW1
Cherek, H; Gryczynski, I; Joshi, N; Lakowicz, JR; Szmacinski, H1
Berman, HA; Nowak, MW1
Karkaria, CE; Rosen, BP; Steiner, RF1
Deléage, G; Di Pietro, A; Divita, G; Gautheron, DC; Roux, B1
Pain, RH; Varley, PG1
Ilich, P; Prendergast, FG1
Narasimhulu, S2
Drake, SK; Frerman, FE; Loehr, JP; Watmough, NJ1
Barkley, MD; Laine, RA; Zhu, BC1
Betley, MJ; Singh, BR1
Chang, LS; Yang, CC1
Auclair, F; Mantsch, HH; Surewicz, K; Surewicz, WK1
Eftink, MR; Wasylewski, Z1
Berger, JW; Vanderkooi, JM1
Deibel, MR; Epps, DE; Yem, AW1
D'Onofrio, M; Giganti, MG; Grimaldi, S; Pascale, E; Pozzi, D; Verna, R1
Steinberg, M; Tyson, PA2
Hug, DH; O'Donnell, PS1
Stryjewski, W; Wasylewski, Z1
Chen, LX; Fleming, GR; Longworth, JW1
Eftink, MR; Hagaman, KA3
Eftink, MR; Ghiron, CA2
Baudet, S; Jullien, M; Le Bras, G; Rodier, F1
Haase, FC; Kumar, GK; Phillips, NF; Wood, HG1
Chai, YG; Lee, J; Robinson, GW; Singh, BR; Song, PS1
Carlson, W; Epps, DE; Heinrikson, R; Hui, J; Poorman, R1
Borkman, RF; Phillips, SR1
Augusteyn, RC; Putilina, T; Seifert, R1
Lerman, S; Moran, M1
Chang, GG; Chen, YH; Lee, HJ1
Cherek, H; Gryczynski, I; Johnson, ML; Joshi, N; Lakowicz, JR1
Gryczynski, I; Johnson, ML; Joshi, NB; Lakowicz, JR; Szmacinski, H1
Behnke, WD; Hundley, P; McIntyre, JC1
Borkman, RF; Phillips, SR; Wilson, LJ1
Beltramini, M; Lerch, K1
Torgerson, PM1
Armenian, AG; Gasparian, VK; Mardanian, SS; Nalbandian, RM1
Giménez-Gallego, G; Lozano, RM; Muñoz-Willery, I; Núñez De Castro, I; Pineda-Lucena, A; Zazo, M1
Haavik, J; Knappskog, PM1
Chakrabarti, A; Majee, S1
Merrill, AR; Palmer, LR; Szabo, AG1
Bandyopadhyay, S; Banik, U; Bhattacharyya, B; Mandal, NC; Roy, S1
Anzenbacher, P; Balny, C; Lange, R; Maurin, L; Müller, S1
Hedstrom, J; Norman, JA; Prendergast, FG; Punyiczki, M; Rosenberg, A; Somogyi, B1
Gryczynski, I; Johnson, ML; Kuśba, J; Lakowicz, JR; Zelent, B2
Bujalowski, W; Klonowska, MM1
Chang, YC; Ludescher, RD2
Augusteyn, RC; Chandrasekher, G; Ghiggino, KP; Vassett, P1
Friedman, JM; Harrington, JP; Hirsch, RE; Vidugiris, GJ1
Manabe, K; Nakazawa, M; Song, PS; Wells, TA1
English, AM; Ferreira-Rajabi, L; Fox, T; Hill, BC1
Bhattacharyya, A; Bhattacharyya, B; Roy, S1
Cardemil, E; Encinas, MV; Goldie, H; Rojas, MC1
Augusteyn, RC; Ghiggino, KP; Putilina, T1
Consler, TG; Kaback, HR; Weitzman, C1
Billheimer, JT; Colles, SM; McLean, LR; Moncecchi, D; Myers-Payne, SC; Schroeder, F; Woodford, JK1
Małecki, J; Wasylewski, M; Wasylewski, Z1
Mishra, VK; Palgunachari, MN1
Itoh, Y; Nagase, H; Stack, MS; Young, TN1
Helmkamp, GM; Tremblay, JM; Voziyan, PA; Yarbrough, LR1
Drwiega, M; Kaszycki, P; Wasylewski, Z1
Gabrielsen, OS; Hegvold, AB1
Bousquet, JA; Ettner, N1
Cui, D; Lin, Q; Wang, Q1
Fidler, V; Fleming, GR; Hof, M1
Craescu, CT; Gallay, J; Rouviere, N; Vincent, M1
Cheung, HC; Dong, WJ; She, M; Umeda, PK1
Awasthi, YC; Bandorowicz-Pikuła, J; Pikuła, S; Wrzosek, A1
Gao, P; Sun, YQ; Yan, BX1
Cester, N; Curatola, A; Fumelli, P; Kotyk, A; Kvasnicka, P; Mazzanti, L; Rabini, RA; Staffolani, R; Zolese, G1
Bieth, JG; Cadène, M; Mély, Y; Sylte, I1
Don, Y; Li, H; Liu, N; Wu, H; Yang, K; Zhang, Y1
Denhardt, DT; Lackland, H; Ludescher, RD; Rajan, SS1
Frère, JM; Guillaume, G; Lejeune, A; Pain, RH; Schmid, FX; Vanhove, M; Virden, R1
Kosk-Kosicka, D; Lopez, MM1
Blandin, P; Desmadril, M; Garcia, P; Mérola, F; Minard, P; Receveur, V1
Breukink, E; de Kruijff, B; Demel, RA; Kuipers, OP; Siezen, RJ; van Dalen, A; van Kraaij, C1
Brennan, JD; Hogue, CW; Zheng, L1
Bazin, M; Brochon, JC; Jurado, J; Kuznetsov, SV; Laval, J; Santus, R; Sidorkina, OM; Tauc, P1
Aleksiev, B; Betzel, C; Dolashka, P; Genov, N; Mancheva, I; Rajashankar, KR1
Gallay, J; Lewit-Bentley, A; Sopkova, J; Takahashi, M; Vincent, M1
Alvarez, C; Campos, AM; Lanio, ME; Lissi, EA; Martinez, D; Morera, V; Pazos, IF1
Busti, P; Delorenzi, NJ; Gatti, CA1
Komath, SS; Padma, P; Swamy, MJ1
Amrani, A; Azarkan, M; Looze, Y; Nijs, M; Smolders, N; Vincentelli, J; Zerhouni, S1
Park, HS; Park, JW1
Li, J; Meighen, EA; Szittner, R1
Ajtai, K; Burghardt, TP; Park, S1
Bain, AJ; Bryant, J; Chadborn, N; O'Shea, P1
Imoto, T; Nishimoto, E; Yamasaki, N; Yamashita, S1
Kay, CM; Kiss, RS; Ryan, RO1
Kleinschmidt, JH; Tamm, LK1
Das, I; Datta, AK; Ghosh, M; Sinha, KM1
Biktashev, AG; Khaitlina, SY; Kuznetsova, IM; Turoverov, KK1
Bułaj, G; Dobryszycki, P; Kochman, M; Rymarczuk, M1
Dobryszycki, P; Gapiński, J; Kochman, M; Rymarczuk, M1
Ling, V; Ruysschaert, JM; Shapiro, AB; Sonveaux, N; Vigano, C1
Engelborghs, Y; Gastmans, M; Volckaert, G1
Merrill, AR; Tory, MC1
Guzman, G; Miller, TE; Moncrieffe, MC; Potter, JD; Prendergast, FG; Venyaminov, SY1
Masaki, K; Mizuguchi, M; Nitta, K1
Biktashev, AG; Khaitlina, SY; Kuznetsova, IM; Turoverov, KK; Uversky, VN; Vassilenko, KS1
Dirr, HW; Wallace, LA2
Behere, DV; Deva, MS1
Anderluh, G; Barlic, A; MaCek, P; Malovrh, P; Menestrina, G; Podlesek, Z1
France, RM; Grossman, SH1
Bandyopadhyay, S; Deb, S; Roy, S1
Senior, AE; Weber, J1
Kay, C; Prenner, EJ; Ryan, RO; Weers, PM1
Barnes, JA; Gomes, AV; Vogel, HJ1
Burghardt, TP; Park, S1
Mitra, S; Sau, AK1
Gelamo, EL; Tabak, M1
Liu, R; Sharom, FJ; Siemiarczuk, A1
Fidy, J; Laberge, M; Polgár, L; Szeltner, Z; Tölgyesi, F; Ullrich, B1
Abugo, O; Collins, JH; Digel, J; Gryczynski, Z; Kobayashi, T; Lakowicz, JR1
Duncan, MW; Golding, J; Henderson, T; Hochgrebe, T; Hou, JY; Lynch, G; Poljak, A; Zoellner, H1
Choi, G; Choi, KY; Ha, NC; Hong, BH; Kim, MS; Oh, BH1
D'Auria, S; Di Cesare, N; Gryczynski, I; Lakowicz, JR; Rossi, M1
Beal, PA; Stephens, OM; Yi-Brunozzi, HY1
Chen, CH; Martin, DL; Rust, E1
Corbalán-García, S; del Mar Martínez-Senac, M; Gómez-Fernández, JC1
Chang, CC; Chang, LS; Lin, SR; Wang, JJ1
Counts Gerber, N; Kosarikov, DN; Lee, JM; Uversky, VN1
Pinheiro, TJ; Sanghera, N1
Bhattacharyya, D; Brahma, A; Mukherjee, C; Nayar, S1
Kasturi, SR; Kuchroo, K; Maity, H1
Cioni, P; Strambini, GB1
Bandyopadhyay, S; Bose, S; Deb, S; Roy, S1
Bera, AK; Bernhardt, R; Fischer, B; Hannemann, F; Lisurek, M; Teuchner, K1
Breukink, E; de Kruijff, B; van Heusden, HE1
Jarori, GK; Maity, H1
Cardemil, E; Espinosa, V; Kettlun, AM; Valenzuela, MA; Zanocco, A1
Chatterji, D; Ghosh, P; Ramakrishnan, C1
Bettati, S; Campanini, B; Cook, PF; Hazlett, TL; Mozzarelli, A; Raboni, S; Vaccari, S; Zhang, L1
Federkeil, SL; Jickling, G; Turner, RJ; Winstone, TL1
De Maeyer, M; Engelborghs, Y; Hao, Q; Hellings, M; Peumans, WJ; Van Damme, EJ; Verheyden, S1
Broos, J; Gabellieri, E; Jackson, JB; Strambini, GB; van Boxel, GI1
Genov, N; Idakieva, K; Parvanova, K; Todinova, S1
Arellano, JB; Balsera, M; De Las Rivas, J; Devos, D; Pazos, F; Valencia, A1
Hidaka, H; Iwamoto, Y; Muramatsu, T; Oda, T1
Fraaije, MW; Janssen, DB; Lutje Spelberg, JH; Tang, L; van Merode, AE1
Kadoya, A; Miyake, H; Ohyashiki, T1
Iannuzzi, C; Irace, G; Malmo, C; Sirangelo, I1
Kusior, D; Olszowska, E; Olszowski, S; Piwowarczyk, M; Stelmaszynska, T1
Bravo, A; Gómez, I; Miranda-CassoLuengo, R; Muñoz-Garay, C; Rausell, C; Rudiño-Piñera, E; Soberón, M1
Hahm, KS; Kim, JI; Kim, Y; Lim, SS; Shin, SY; Song, YM; Yang, ST1
Jung, SJ; Kim, HE; Lee, BJ; Seo, MD; Won, HS1
Canters, GW; Cioni, P; de Waal, E; Strambini, GB1
Andrade, SM; Carvalho, TI; Costa, SM; Viseu, MI1
Bârzu, O; Gallay, J; Gilles, AM; Li de la Sierra, IM; Munier-Lehmann, H; Renouard, M; Sakamoto, H; Vincent, M1
Fang, H; Wang, G; Xia, X1
Esbjörner, EK; Goksör, M; Lincoln, P; Nordén, B; Persson, D; Thorén, PE1
Cheng, Z; Ching Lee, J; Daly, TJ; Herman, P; Surendran, R1
Ahmad, B; Ashraf, MT; Khan, RH; Naseem, F1
Gensch, T; Hellingwerf, KJ; Hendriks, J1
Kinne, RK; Kipp, H; Raja, MM1
Fernández, M; Fuentes, L; Oyola, J; Quiñones, E1
Davidson, WS; Horace, EM; Jandacek, RJ; Maiorano, JN1
Driessen, AJ; Gbaguidi, B; Konings, WN; Mazurkiewicz, P; Ruysschaert, JM; Vigano, C1
Kazakov, VI; Kuznetsova, IM; Shavlovsky, MM; Stepanenko, OV; Turoverov, KK; Uversky, VN; Verkhusha, VV1
Bren, N; Burghardt, TP; Gao, F; Hansen, S; Henchman, RH; McCammon, JA; Sine, SM; Taylor, P1
An, J; Bao, JK; Chen, F; Gao, S; Gu, Y; Wu, CF; Wu, QQ; Yu, Y1
Japelj, B; Jerala, R; Majerle, A; Pristovsek, P1
Nicholls, IA; Olofsson, L; Wikman, S1
Igarashi, K; Kawano, K; Matsubara, K; Matsuura, A; Mizuguchi, M; Mori, Y; Saitoh, T; Shinoda, H; Shinohara, Y; Takeuchi, M1
Chen, J; Pang, Y; Wu, P; Zhu, H1
den Blaauwen, T; Driessen, AJ; Natale, P; van der Does, C1
Berger, CL; Chrin, LR; Gaffney, DP; Robertson, CI1
Catalano, CE; Gaussier, H; Maluf, NK; Ortega, ME1
Chattopadhyay, A; Kelkar, DA; Rawat, SS1
Chen, A; Greenfield, NJ; He, H; Nair, SK; Thomas, T; Thomas, TJ1
Hemminga, MA; Hesselink, RW; Koehorst, RB; Nazarov, PV1
Crespo, JG; Lima, JC; Portugal, CA1
Ahmad, B; Ansari, MA; Khan, RH; Sen, P1
Jenei, A; Mátyus, L; Szöllosi, J1
Bodner, N; Dusa, A; Edridge, S; Fink, AL; Hong, DP; Kaylor, J1
Ceulemans, A; De Maeyer, M; Engelborghs, Y; Hellings, M; Moors, SL1
Bankston, JR; Glaaser, IW; Kass, RS; Liu, H; Tateyama, M1
Russell, PL; Sharom, FJ1
Chaudhuri, TK; Deb, JK; Jana, S1
Chattopadhyay, A; Kelkar, DA1
Acebal, C; Arroyo, M; Campillo, N; Castillón, MP; de la Mata, I; García, JL; Hormigo, D; Menéndez, M1
Arora-Sharawat, A; Chattopadhyay, A1
Gaikwad, SM; Shashidhara, KS1
Alston, RW; Grimsley, GR; Lasagna, M; Pace, CN; Reinhart, GD; Scholtz, JM1
Fedorov, A; Hemminga, MA; Hesselink, RW; Prieto, M1
Domanov, Y; Kinnunen, PK; Kontinen, VP; Pietiäinen, M; Sood, R1
He, XW; Li, WY; Qin, L; Zhang, YK1
Dong, A; Ji, C; Kong, J; Li, H; Ou, Y; Shen, X; Tao, W; Yu, S1
Herman, P; Vecer, J1
Browne, H; Falanga, A; Fattorusso, R; Galdiero, M; Galdiero, S; Isernia, C; Pedone, C; Raiola, L; Vitiello, M1
Cordeiro-da-Silva, A; de Castro, B; Gameiro, P; Lima, SA1
Gonnelli, M; Strambini, GB4
Anderson, SR; Broderick, D; Deinzer, ML; Harder, ME; Leid, M; Malencik, DA; Schimerlik, MI; Yan, X1
Bourbon-Freie, A; Dub, RE; Lowe, ME; Xiao, X1
Boone, TC; Carpenter, JF; Kerwin, BA; Mason, BD; Roy, S; Schöneich, CS1
Biverståhl, H; Bodor, A; Lind, J; Mäler, L1
Narahari, A; Swamy, MJ1
Jung, HH; Kim, HJ; Kim, JI; Lee, JY; Lee, SK; Shin, SY; Yang, ST1
Gaikwad, S; Gowda, NM; Kumar, A; Pundle, A1
Ju, H; Lei, J; Ouyang, R; Qu, P1
de Foresta, B; Gallay, J; Garrigos, M; Vincent, M1
Blom, SM; Jensen, HS; Schmitt, N1
Ansari, MA; Anwar, T; Atif, SM; Iqbal, A; Kashif, M; Khan, N; Owais, M; Rehan, M; Zubair, S1
Falanga, A; Galdiero, M; Galdiero, S; Isernia, C; Pedone, C; Raiola, L; Russo, L; Vitiello, M1
Chattopadhyay, A; Chaudhuri, A; Haldar, S; Kelkar, DA1
Wang, SS; Wen, WS1
Daubner, SC; Fitzpatrick, PF; Lasagna, M; Reinhart, GD; Wang, S1
Chen, Y; Erickson, HP1
Bauer, CE; Dragnea, V; Gardner, KH; Wu, Q; Yuan, H1
Chandra, V; Dave, S; Gupta, P; Mahajan, S1
Cantisani, M; D'Errico, G; Falanga, A; Galdiero, M; Galdiero, S; Perillo, E; Tarallo, R; Vitiello, G; Vitiello, M1
Ghosh, G; Mandal, DK1
Ho, J; Wong, KF1
Breukink, E; Irving, N; Mantovani, HC; Paiva, AD1
Iram, A; Naeem, A1
Ahmad, E; Ashraf, R; Bhushan, B; Chaturvedi, SK; Khan, JM; Khan, RH; Qadeer, A; Rabbani, G1
Amoussouvi, A; Haralampiev, I; Herrmann, A; Stöckl, M; Wietek, J1
He, F; Joshi, SB; Kerwin, BA; Middaugh, CR; Sahni, N; Thakkar, SV; Volkin, DB1
Mandal, DK; Sen, D1
Podile, AR; Swamy, MJ; Tarafdar, PK; Vedantam, LV1
Auton, M; Blancas-Mejia, LM; Madde, P; Tischer, A1
Klinman, JP; Meadows, CW; Ou, R1
Ahmad, A; Azmi, S; Ghosh, JK; Kumar, A; Mishra, NN; Shukla, PK; Srivastava, S; Tripathi, JK1
Wang, Y; Yu, LP; Zhang, R1
Dong, W; Ma, L; Shang, D; Sun, L; Sun, Y1
Chattopadhyay, K; Ghosh, R; Ghosh, S; Mukherjee, M1
Hilt, S; Longo, ML; Risbud, SH; Voss, JC; Zeno, WF1
Chaari, A; Chevillot-Biraud, A; Fahy, C; Rholam, M1
Breydo, L; Miti, T; Muschol, M; Niyangoda, C; Uversky, V1
Ghosh, R; Ghosh, S; Mukherjee, M; Mukherjee, P; Mukhopadhyay, TK; Roy, P; Sardar, PS1

Reviews

2 review(s) available for acrylamide and tryptophan

ArticleYear
Fluorescence quenching studies with proteins.
    Analytical biochemistry, 1981, Jul-01, Volume: 114, Issue:2

    Topics: Acetamides; Acrylamide; Acrylamides; Alcohol Oxidoreductases; Azurin; Chemical Phenomena; Chemistry, Physical; Ethylene Chlorohydrin; Fluorescence; Hydrogen Peroxide; Indoles; Kinetics; Liver; Luminescent Measurements; Mathematics; Plant Proteins; Proteins; Pyridinium Compounds; Sodium Iodide; Succinimides; Tryptophan; Tyrosine

1981
Frequency domain fluorometry with pulsed light-emitting diodes.
    Annals of the New York Academy of Sciences, 2008, Volume: 1130

    Topics: Acrylamide; Computers; Equipment Design; Fluorescence Polarization; Fluorometry; Lasers; Light; NAD; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Time Factors; Tryptophan

2008

Other Studies

244 other study(ies) available for acrylamide and tryptophan

ArticleYear
Conformational stability of bovine alpha-crystallin. Evidence for a destabilizing effect of ascorbate.
    The Biochemical journal, 1992, Oct-01, Volume: 287 ( Pt 1)

    Topics: Acrylamide; Acrylamides; Animals; Ascorbic Acid; Cattle; Crystallins; Guanidine; Guanidines; Hot Temperature; Hydrogen-Ion Concentration; In Vitro Techniques; Iodides; Light; Nephelometry and Turbidimetry; Protein Conformation; Protein Denaturation; Scattering, Radiation; Spectrometry, Fluorescence; Tryptophan; Urea

1992
Yeast 5S rRNA binding to ribosomal protein L1a alters the fluorescence of tryptophan residues lying outside the binding site.
    Biochimie, 1992, Volume: 74, Issue:11

    Topics: Acrylamide; Acrylamides; Binding Sites; Fluorescence; Fungal Proteins; Potassium Iodide; Protein Binding; Ribosomal Proteins; RNA-Binding Proteins; RNA, Ribosomal, 5S; Saccharomyces cerevisiae; Tryptophan

1992
Cofactor and DNA interactions in EcoRI DNA methyltransferase. Fluorescence spectroscopy and phenylalanine replacement for tryptophan 183.
    The Journal of biological chemistry, 1992, Sep-15, Volume: 267, Issue:26

    Topics: Acrylamide; Acrylamides; Base Sequence; DNA; Fluorescence Polarization; Genetic Vectors; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; S-Adenosylmethionine; Site-Specific DNA-Methyltransferase (Adenine-Specific); Tryptophan

1992
Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching.
    European biophysics journal : EBJ, 1991, Volume: 19, Issue:3

    Topics: Acrylamide; Acrylamides; Adrenocorticotropic Hormone; Amino Acid Sequence; Birefringence; Fluorescence Polarization; Macromolecular Substances; Micrococcal Nuclease; Molecular Sequence Data; Molecular Structure; Oligopeptides; Oxygen; Plant Proteins; Protein Conformation; Ribonuclease T1; Spectrometry, Fluorescence; Tryptophan

1991
Fluorescence studies on the interactions of myelin basic protein in electrolyte solutions.
    Biochemistry, 1991, Jul-30, Volume: 30, Issue:30

    Topics: Acrylamide; Acrylamides; Animals; Brain Chemistry; Cattle; Diffusion; Electrolytes; Fluorescence; Macromolecular Substances; Myelin Basic Protein; Protein Conformation; Spectrum Analysis; Tryptophan; Urea

1991
Ligand interactions in the ArsA protein, the catalytic component of an anion-translocating adenosinetriphosphatase.
    Biochemistry, 1991, Mar-12, Volume: 30, Issue:10

    Topics: Acrylamide; Acrylamides; Adenosine Triphosphatases; Adenosine Triphosphate; Anions; Arsenite Transporting ATPases; Catalysis; Escherichia coli; Fluorescence Polarization; Ion Pumps; Ligands; Magnesium; Multienzyme Complexes; Protein Conformation; Tryptophan

1991
Intrinsic tryptophan fluorescence of Schizosaccharomyces pombe mitochondrial F1-ATPase. A powerful probe for phosphate and nucleotide interactions.
    Biochemistry, 1991, Apr-02, Volume: 30, Issue:13

    Topics: Acrylamide; Acrylamides; Adenosine Diphosphate; Adenosine Triphosphate; Guanidine; Guanidines; Iodides; Macromolecular Substances; Mitochondria; Protein Conformation; Proton-Translocating ATPases; Schizosaccharomyces; Spectrometry, Fluorescence; Tryptophan

1991
Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus.
    Journal of molecular biology, 1991, Jul-20, Volume: 220, Issue:2

    Topics: Acrylamide; Acrylamides; Enzyme Stability; Hot Temperature; Kinetics; Phosphoglycerate Kinase; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Thermodynamics; Thermus; Tryptophan

1991
Electronic states of the indole-acrylamide molecular pair.
    Photochemistry and photobiology, 1991, Volume: 53, Issue:4

    Topics: Acrylamide; Acrylamides; Electrochemistry; Indoles; Photochemistry; Spectrometry, Fluorescence; Tryptophan

1991
Inhibition of substrate binding to the adrenal cytochrome P450C-21 by acrylamide and its implications for solvent accessibility of the binding site in the microsomes.
    Biochemistry, 1991, Sep-24, Volume: 30, Issue:38

    Topics: 17-alpha-Hydroxyprogesterone; Acrylamide; Acrylamides; Adrenal Cortex; Animals; Binding Sites; Cattle; Hydroxyprogesterones; Intracellular Membranes; Kinetics; Membrane Lipids; Microsomes; Solvents; Spectrometry, Fluorescence; Steroid 21-Hydroxylase; Tryptophan

1991
Tryptophan fluorescence in electron-transfer flavoprotein:ubiquinone oxidoreductase: fluorescence quenching by a brominated pseudosubstrate.
    Biochemistry, 1991, Feb-05, Volume: 30, Issue:5

    Topics: Acrylamide; Acrylamides; Animals; Cesium; Chlorides; Electron-Transferring Flavoproteins; Fatty Acid Desaturases; Flavoproteins; Hydrogen-Ion Concentration; In Vitro Techniques; Iron-Sulfur Proteins; Kinetics; Multienzyme Complexes; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Sodium Iodide; Spectrometry, Fluorescence; Structure-Activity Relationship; Submitochondrial Particles; Swine; Tryptophan; Ubiquinone; Urea

1991
Intrinsic tryptophan fluorescence measurements suggest that polylactosaminyl glycosylation affects the protein conformation of the gelatin-binding domain from human placental fibronectin.
    European journal of biochemistry, 1990, May-20, Volume: 189, Issue:3

    Topics: Acrylamide; Acrylamides; Amino Sugars; beta-Galactosidase; Binding Sites; Chymotrypsin; Electrophoresis, Polyacrylamide Gel; Female; Fibronectins; Gelatin; Glycoproteins; Glycoside Hydrolases; Glycosylation; Humans; Mathematics; Placenta; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1990
Comparative structural analysis of staphylococcal enterotoxins A and E.
    The Journal of biological chemistry, 1989, Mar-15, Volume: 264, Issue:8

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Chemical Phenomena; Chemistry, Physical; Circular Dichroism; Enterotoxins; Epitopes; Molecular Sequence Data; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1989
Assessment of the role of tryptophan residues in phospholipase A2 by fluorescence quenching.
    International journal of biological macromolecules, 1989, Volume: 11, Issue:1

    Topics: Acrylamide; Acrylamides; Binding Sites; Elapid Venoms; Fluorescence; Iodides; Phospholipases A; Phospholipases A2; Substrate Specificity; Tryptophan

1989
Interaction of Shigella toxin with globotriaosyl ceramide receptor-containing membranes: a fluorescence study.
    Biochemical and biophysical research communications, 1989, Apr-14, Volume: 160, Issue:1

    Topics: Acrylamide; Acrylamides; Bacterial Toxins; Dimyristoylphosphatidylcholine; Globosides; Glycosphingolipids; Lipid Bilayers; Liposomes; Phosphatidylcholines; Protein Conformation; Shiga Toxins; Shigella dysenteriae; Spectrometry, Fluorescence; Trihexosylceramides; Tryptophan

1989
Fluorescence lifetime and solute quenching studies with the single tryptophan containing protein parvalbumin from codfish.
    Biochemistry, 1989, Jan-10, Volume: 28, Issue:1

    Topics: Acrylamide; Acrylamides; Animals; Calcium; Fishes; Kinetics; Muscle Proteins; Parvalbumins; Spectrometry, Fluorescence; Tryptophan

1989
Characterization of lens alpha-crystallin tryptophan microenvironments by room temperature phosphorescence spectroscopy.
    Biochemistry, 1989, Jun-27, Volume: 28, Issue:13

    Topics: Acrylamide; Acrylamides; Crystallins; Guanidine; Guanidines; Iodides; Luminescent Measurements; Nitrites; Protein Conformation; Protein Denaturation; Spectrum Analysis; Temperature; Thermodynamics; Tryptophan; Urea

1989
Characterization of the tryptophan environments of interleukins 1 alpha and 1 beta by fluorescence quenching and lifetime measurements.
    Archives of biochemistry and biophysics, 1989, Nov-15, Volume: 275, Issue:1

    Topics: Acrylamide; Acrylamides; Cesium; Electrophoresis, Polyacrylamide Gel; Humans; Interleukin-1; Iodides; Kinetics; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

1989
Effect of ouabain binding on the fluorescent properties of the Na+/K+-ATPase.
    Biochimica et biophysica acta, 1988, Sep-15, Volume: 944, Issue:1

    Topics: Acrylamide; Acrylamides; Animals; Fluorescence; Guanidine; Guanidines; Hydrogen-Ion Concentration; Iodides; Ouabain; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Swine; Tryptophan

1988
Quenching of the tryptophan fluorescence of Na,K-ATPase with acrylamide.
    Progress in clinical and biological research, 1988, Volume: 268A

    Topics: Acrylamide; Acrylamides; Animals; Chymotrypsin; Dogs; Kidney; Kinetics; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Tryptophan

1988
Tryptophanyl fluorescence quenching of urocanase from Pseudomonas putida by acrylamide, cesium, iodide, and imidazolepropionate.
    Photochemistry and photobiology, 1985, Volume: 42, Issue:2

    Topics: Acrylamide; Acrylamides; Cesium; Hydro-Lyases; Imidazoles; Iodides; Kinetics; Pseudomonas; Spectrometry, Fluorescence; Tryptophan; Urocanate Hydratase

1985
The resolution of heterogeneous fluorescence of multitryptophan-containing proteins studied by a fluorescence-quenching method.
    European journal of biochemistry, 1986, Aug-01, Volume: 158, Issue:3

    Topics: Acrylamide; Acrylamides; Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Fluorescence; Horses; Muramidase; Phosphoglycerate Kinase; Protein Conformation; Proteins; Tryptophan; X-Ray Diffraction

1986
Accessibility of tryptophan residues in Na,K-ATPase.
    The Journal of biological chemistry, 1987, Apr-05, Volume: 262, Issue:10

    Topics: Acrylamide; Acrylamides; Adenosine Diphosphate; Animals; Chymotrypsin; Dogs; In Vitro Techniques; Ouabain; Potassium; Protein Conformation; Protein Denaturation; Sodium; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Tryptophan

1987
Picosecond time-resolved fluorescence of ribonuclease T1. A pH and substrate analogue binding study.
    Biophysical journal, 1987, Volume: 51, Issue:6

    Topics: Acrylamide; Acrylamides; Binding Sites; Endoribonucleases; Fluorescence Polarization; Guanine Nucleotides; Guanosine Monophosphate; Kinetics; Protein Binding; Protein Conformation; Ribonuclease T1; Spectrometry, Fluorescence; Time Factors; Tryptophan; X-Ray Diffraction

1987
Viscosity dependence of the solute quenching of the tryptophanyl fluorescence of proteins.
    Biophysical chemistry, 1986, Dec-31, Volume: 25, Issue:3

    Topics: Acrylamide; Acrylamides; Glucagon; Parvalbumins; Protein Conformation; Proteins; Ribonuclease T1; Solvents; Spectrometry, Fluorescence; Tryptophan; Viscosity

1986
Frequency domain measurements of the fluorescence lifetime of ribonuclease T1.
    Biophysical journal, 1987, Volume: 52, Issue:3

    Topics: Acrylamide; Acrylamides; Aspergillus oryzae; Calorimetry; Endoribonucleases; Kinetics; Ribonuclease T1; Spectrometry, Fluorescence; Time Factors; Tryptophan

1987
Allosteric transition of aspartokinase I-homoserine dehydrogenase I studied by time-resolved fluorescence.
    Biochimie, 1988, Volume: 70, Issue:12

    Topics: Acrylamide; Acrylamides; Allosteric Regulation; Aspartokinase Homoserine Dehydrogenase; Energy Transfer; Escherichia coli; Fluoroimmunoassay; Multienzyme Complexes; Protein Conformation; Quantum Theory; Spectrometry, Fluorescence; Threonine; Tryptophan

1988
Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase.
    Biochemistry, 1988, Aug-09, Volume: 27, Issue:16

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Binding Sites; Carboxyl and Carbamoyl Transferases; Dinitrobenzenes; Molecular Sequence Data; Propionibacterium; Protein Conformation; Pyruvates; Pyruvic Acid; Spectrometry, Fluorescence; Sulfenic Acids; Transferases; Tryptophan

1988
A photoreversible conformational change in 124 kDa Avena phytochrome.
    Biochimica et biophysica acta, 1988, Dec-07, Volume: 936, Issue:3

    Topics: Acrylamide; Acrylamides; Anions; Cations, Monovalent; Cesium; Chlorides; Edible Grain; Fluorescence; Fluorescent Dyes; Light; Phytochrome; Plant Proteins; Potassium Iodide; Protein Conformation; Seeds; Spectrometry, Fluorescence; Tryptophan

1988
Quenching of tryptophanyl fluorescence of bovine adrenal P-450C-21 and inhibition of substrate binding by acrylamide.
    Biochemistry, 1988, Feb-23, Volume: 27, Issue:4

    Topics: Acrylamide; Acrylamides; Adrenal Cortex; Animals; Cattle; Kinetics; Microsomes; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Steroid 21-Hydroxylase; Steroid Hydroxylases; Tryptophan

1988
Inaccessibility of tryptophan residues of recombinant human renin to quenching agents.
    The Journal of biological chemistry, 1987, Aug-05, Volume: 262, Issue:22

    Topics: Acrylamide; Acrylamides; Cesium; Chlorides; Fluorescence; Glycosylation; Humans; Iodides; Protein Conformation; Protein Denaturation; Recombinant Proteins; Renin; Spectrometry, Fluorescence; Tryptophan

1987
Fluorescence quenching studies of the structures of calf gamma-II, III, and IV crystallins.
    Current eye research, 1988, Volume: 7, Issue:1

    Topics: Acrylamide; Acrylamides; Animals; Cattle; Chemical Phenomena; Chemistry; Circular Dichroism; Crystallins; Iodides; Spectrometry, Fluorescence; Tryptophan

1988
Quenching of tryptophan fluorescence in bovine lens proteins by acrylamide and iodide.
    Current eye research, 1988, Volume: 7, Issue:3

    Topics: Acrylamide; Acrylamides; Animals; Cattle; Crystallins; Iodides; Oxidation-Reduction; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1988
Acrylamide and iodide fluorescence quenching studies on whole human lenses and their protein extracts.
    Current eye research, 1988, Volume: 7, Issue:4

    Topics: Acrylamide; Acrylamides; Adolescent; Adult; Aged; Aging; Child; Child, Preschool; Crystallins; Fluorescence; Humans; Iodides; Lens, Crystalline; Magnetic Resonance Spectroscopy; Middle Aged; Tryptophan; Ultraviolet Rays

1988
Fluorescence studies on the dissociation and denaturation of pigeon liver malic enzyme.
    Biochimica et biophysica acta, 1988, Jul-20, Volume: 955, Issue:2

    Topics: Acrylamide; Acrylamides; Algorithms; Animals; Columbidae; Fluorescence; Guanidine; Guanidines; Liver; Malate Dehydrogenase; Molecular Weight; Protein Denaturation; Tryptophan

1988
Enhanced resolution of fluorescence anisotropy decays by simultaneous analysis of progressively quenched samples. Applications to anisotropic rotations and to protein dynamics.
    Biophysical journal, 1987, Volume: 51, Issue:5

    Topics: Acrylamide; Acrylamides; Bee Venoms; Fluorescence Polarization; Indoles; Melitten; Propylene Glycol; Propylene Glycols; Protein Conformation; Tryptophan

1987
Diffusion coefficients of quenchers in proteins from transient effects in the intensity decays.
    The Journal of biological chemistry, 1987, Aug-15, Volume: 262, Issue:23

    Topics: Acrylamide; Acrylamides; Diffusion; Fluorescence; Fluorometry; Micrococcal Nuclease; Oxygen; Tryptophan

1987
The role of aromatic side chain residues in micelle binding by pancreatic colipase. Fluorescence studies of the porcine and equine proteins.
    The Biochemical journal, 1987, Aug-01, Volume: 245, Issue:3

    Topics: Acrylamide; Acrylamides; Animals; Binding Sites; Cesium; Chlorides; Colipases; Deoxycholic Acid; Horses; Kinetics; Micelles; Pancreas; Potassium Iodide; Protein Binding; Proteins; Spectrometry, Fluorescence; Structure-Activity Relationship; Swine; Taurodeoxycholic Acid; Tryptophan

1987
Acrylamide and iodide fluorescence quenching as a structural probe of tryptophan microenvironment in bovine lens crystallins.
    Current eye research, 1986, Volume: 5, Issue:8

    Topics: Acrylamide; Acrylamides; Animals; Cattle; Chemical Phenomena; Chemistry; Crystallins; Fluorescence; Iodides; Models, Biological; Tryptophan

1986
Fluorescence lifetime and anisotropy studies with liver alcohol dehydrogenase and its complexes.
    Biochemistry, 1986, Oct-21, Volume: 25, Issue:21

    Topics: Acrylamide; Acrylamides; Alcohol Dehydrogenase; Animals; Fluorescence Polarization; Horses; Indoles; Kinetics; Liver; NAD; Protein Binding; Spectrometry, Fluorescence; Tryptophan

1986
Fluorescence quenching of the buried tryptophan residue of cod parvalbumin.
    Biophysical chemistry, 1985, Volume: 22, Issue:3

    Topics: Acrylamide; Acrylamides; Animals; Fishes; Muscle Proteins; Parvalbumins; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1985
Fluorescence properties of Neurospora tyrosinase.
    The Biochemical journal, 1982, Jul-01, Volume: 205, Issue:1

    Topics: Acrylamide; Acrylamides; Anilino Naphthalenesulfonates; Binding Sites; Catechol Oxidase; Energy Transfer; Fluorescent Dyes; Monophenol Monooxygenase; Neurospora; Neurospora crassa; Potassium Iodide; Spectrometry, Fluorescence; Tryptophan

1982
Tryptophan emission from myosin subfragment 1: acrylamide and nucleotide effect monitored by decay-associated spectra.
    Biochemistry, 1984, Jun-19, Volume: 23, Issue:13

    Topics: Acrylamide; Acrylamides; Adenosine Triphosphate; Animals; Kinetics; Muscles; Myosin Subfragments; Myosins; Peptide Fragments; Protein Binding; Rabbits; Spectrometry, Fluorescence; Tryptophan

1984
[Luminescent properties of NADPH: adrenodoxin reductase].
    Biokhimiia (Moscow, Russia), 1984, Volume: 49, Issue:9

    Topics: Acrylamide; Acrylamides; Adrenal Cortex; Animals; Apoenzymes; Ferredoxin-NADP Reductase; Flavin-Adenine Dinucleotide; Fluorescence; Luminescent Measurements; Mitochondria; NADH, NADPH Oxidoreductases; Protein Denaturation; Temperature; Tryptophan; Urea

1984
Effect of low pH and heparin on the structure of acidic fibroblast growth factor.
    European journal of biochemistry, 1994, Jun-01, Volume: 222, Issue:2

    Topics: 3T3 Cells; Acrylamide; Acrylamides; Animals; Cell Division; Fibroblast Growth Factor 1; Heparin; Hydrogen-Ion Concentration; Kinetics; Mice; Models, Structural; Osmolar Concentration; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

1994
Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli.
    Biochemistry, 1995, Sep-19, Volume: 34, Issue:37

    Topics: Acrylamide; Acrylamides; Base Sequence; Biopterins; DNA, Complementary; Escherichia coli; Humans; In Vitro Techniques; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Phenylalanine Hydroxylase; Polymerase Chain Reaction; Recombinant Fusion Proteins; Spectrometry, Fluorescence; Tryptophan

1995
A DNA-binding antitumor antibiotic binds to spectrin.
    Biochemical and biophysical research communications, 1995, Jul-17, Volume: 212, Issue:2

    Topics: Acrylamide; Acrylamides; Animals; DNA; Fluorescence; Goats; Macromolecular Substances; Magnesium; Plicamycin; Protein Conformation; Spectrin; Spectrometry, Fluorescence; Tryptophan

1995
Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state.
    Biochemistry, 1993, Jul-13, Volume: 32, Issue:27

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Colicins; Fluorescence; Genetic Engineering; Ion Channels; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Protein Conformation; Tryptophan

1993
Role of the C-terminal tail region in the self-assembly of lambda-repressor.
    Biochemistry, 1995, Apr-18, Volume: 34, Issue:15

    Topics: Acrylamide; Acrylamides; Amino Acids; DNA-Binding Proteins; Hydrogen-Ion Concentration; Peptide Mapping; Repressor Proteins; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan; Viral Proteins; Viral Regulatory and Accessory Proteins

1995
Interaction of tryptophan residues of cytochrome P450scc with a highly specific fluorescence quencher, a substrate analogue, compared to acrylamide and iodide.
    European journal of biochemistry, 1994, Dec-15, Volume: 226, Issue:3

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Binding Sites; Cholesterol; Cholesterol Side-Chain Cleavage Enzyme; Fluorescence; Fluorescent Dyes; Molecular Sequence Data; Potassium Iodide; Spectrometry, Fluorescence; Tryptophan

1994
Coupling between external viscosity and the intramolecular dynamics of ribonuclease T1: a two-phase model for the quenching of protein fluorescence.
    Biochimica et biophysica acta, 1994, Nov-16, Volume: 1209, Issue:1

    Topics: Acrylamide; Acrylamides; Fluorescence; Glycerol; Models, Chemical; Ribonuclease T1; Spectrometry, Fluorescence; Tryptophan; Viscosity

1994
Distance-dependent fluorescence quenching of tryptophan by acrylamide.
    Photochemistry and photobiology, 1994, Volume: 60, Issue:3

    Topics: Acrylamide; Acrylamides; Kinetics; Mathematics; Models, Theoretical; Spectrometry, Fluorescence; Time Factors; Tryptophan

1994
Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein. Molecular topography of the enzyme.
    The Journal of biological chemistry, 1994, Dec-16, Volume: 269, Issue:50

    Topics: Acrylamide; Acrylamides; Adenine Nucleotides; Bacterial Proteins; Binding Sites; DNA Helicases; DNA Replication; DnaB Helicases; Energy Transfer; Escherichia coli; In Vitro Techniques; Protein Denaturation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan

1994
Local conformation of rabbit skeletal myosin rod filaments probed by intrinsic tryptophan fluorescence.
    Biochemistry, 1994, Mar-01, Volume: 33, Issue:8

    Topics: Acrylamide; Acrylamides; Animals; Fluorescence Polarization; Muscles; Myosins; Protein Conformation; Rabbits; Time Factors; Tryptophan

1994
Probing the microenvironments of tryptophan residues in the monomeric crystallins of the bovine lens.
    Biochimica et biophysica acta, 1994, Mar-16, Volume: 1205, Issue:1

    Topics: Acrylamide; Acrylamides; Crystallins; Potassium Iodide; Spectrometry, Fluorescence; Tryptophan

1994
Alteration of tryptophan fluorescence properties upon dissociation of Lumbricus terrestris hemoglobin.
    Biochimica et biophysica acta, 1994, Apr-13, Volume: 1205, Issue:2

    Topics: Acrylamide; Acrylamides; Animals; Carboxyhemoglobin; Hemoglobins; Hydrogen-Ion Concentration; Oligochaeta; Oxyhemoglobins; Spectrometry, Fluorescence; Tryptophan

1994
Tryptophan fluorescence quenching in rabbit skeletal myosin rod.
    Biophysical chemistry, 1993, Volume: 48, Issue:1

    Topics: Acrylamide; Acrylamides; Animals; Iodides; Muscles; Myosins; Protein Conformation; Protein Structure, Secondary; Rabbits; Solvents; Spectrometry, Fluorescence; Tryptophan

1993
A conformational change associated with the phototransformation of Pisum phytochrome A as probed by fluorescence quenching.
    Biochemistry, 1994, Jan-25, Volume: 33, Issue:3

    Topics: 2-Hydroxy-5-nitrobenzyl Bromide; Acrylamide; Acrylamides; Cesium; Fabaceae; Light; Phytochrome; Plants, Medicinal; Spectrometry, Fluorescence; Thallium; Time Factors; Tryptophan

1994
Quenching of intrinsic fluorescence of yeast cytochrome c peroxidase by covalently- and noncovalently-bound quenchers.
    Biochemistry, 1993, Jul-13, Volume: 32, Issue:27

    Topics: Acrylamide; Acrylamides; Cesium; Cyanides; Cytochrome-c Peroxidase; Fluorescence; Iodides; Ruthenium; Ruthenium Compounds; Saccharomyces cerevisiae; Tryptophan

1993
A study of colchicine tubulin complex by donor quenching of fluorescence energy transfer.
    European journal of biochemistry, 1993, Sep-15, Volume: 216, Issue:3

    Topics: Acrylamide; Acrylamides; Alcohol Dehydrogenase; Animals; Colchicine; Dimethyl Sulfoxide; Energy Transfer; Horses; Liver; NAD; Spectrometry, Fluorescence; Tryptophan; Tubulin

1993
Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phospho enol pyruvate carboxykinases.
    Biochimica et biophysica acta, 1993, Mar-05, Volume: 1162, Issue:1-2

    Topics: Acrylamide; Acrylamides; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Cytosol; Escherichia coli; Fluorescence; Guanosine Triphosphate; Liver; Manganese; Nucleotides; Phosphoenolpyruvate Carboxykinase (GTP); Protein Conformation; Rats; Saccharomyces cerevisiae; Sodium Iodide; Tryptophan

1993
Studies on the location of aromatic amino acids in alpha-crystallin.
    Biochimica et biophysica acta, 1993, Mar-05, Volume: 1162, Issue:1-2

    Topics: Acrylamide; Acrylamides; Amino Acids; Animals; Cattle; Crystallins; Hydrogen-Ion Concentration; Iodides; Protein Conformation; Spectrometry, Fluorescence; Temperature; Tryptophan; Urea

1993
Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change.
    Protein science : a publication of the Protein Society, 1995, Volume: 4, Issue:11

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Anilino Naphthalenesulfonates; Escherichia coli; Escherichia coli Proteins; Iodides; Lactose; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Reagents; Symporters; Tryptophan

1995
Cholesterol interaction with recombinant human sterol carrier protein-2.
    Lipids, 1995, Volume: 30, Issue:9

    Topics: Acrylamide; Acrylamides; Binding Sites; Carrier Proteins; Cholesterol; Circular Dichroism; Drug Interactions; Ergosterol; Fluorometry; Humans; Microsomes; Plant Proteins; Recombinant Proteins; Sterols; Tryptophan

1995
Fluorescence study of Escherichia coli cyclic AMP receptor protein.
    Journal of protein chemistry, 1995, Volume: 14, Issue:5

    Topics: Acrylamide; Acrylamides; Bacterial Proteins; Circular Dichroism; Cyclic AMP; Cyclic AMP Receptor Protein; Escherichia coli; Fluorescence; Iodides; Kinetics; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1995
Interaction of model class A1, class A2, and class Y amphipathic helical peptides with membranes.
    Biochemistry, 1996, Aug-27, Volume: 35, Issue:34

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Apolipoproteins; Calorimetry, Differential Scanning; Chromatography, High Pressure Liquid; Circular Dichroism; Computer Simulation; Gels; Lipid Bilayers; Membrane Lipids; Molecular Sequence Data; Peptides; Phospholipids; Protein Structure, Secondary; Scattering, Radiation; Spectrometry, Fluorescence; Tryptophan

1996
Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation.
    Archives of biochemistry and biophysics, 1996, Sep-01, Volume: 333, Issue:1

    Topics: Acrylamide; Acrylamides; Enzyme Activation; Enzyme Precursors; Female; Fluorescence; Gelatinases; Humans; In Vitro Techniques; Macromolecular Substances; Metalloendopeptidases; Molecular Structure; Phenylmercuric Acetate; Protease Inhibitors; Proteins; Spectrometry, Fluorescence; Tissue Inhibitor of Metalloproteinase-2; Tryptophan

1996
Truncations of the C-terminus have different effects on the conformation and activity of phosphatidylinositol transfer protein.
    Biochemistry, 1996, Sep-24, Volume: 35, Issue:38

    Topics: Acrylamide; Acrylamides; Anilino Naphthalenesulfonates; Animals; Carrier Proteins; Circular Dichroism; Cysteine; Dithionitrobenzoic Acid; Escherichia coli; Kinetics; Membrane Proteins; Mutation; Phosphatidylcholines; Phosphatidylinositols; Phospholipid Transfer Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Deletion; Tryptophan

1996
A fluorescence study of Tn10-encoded tet repressor.
    Journal of protein chemistry, 1996, Volume: 15, Issue:1

    Topics: Acrylamide; Acrylamides; Bacterial Proteins; DNA Nucleotidyltransferases; Escherichia coli; Fluorescence; Helix-Turn-Helix Motifs; Molecular Conformation; Mutation; Potassium Iodide; Repressor Proteins; Spectrometry, Fluorescence; Succinimides; Temperature; Transposases; Tryptophan

1996
The importance of the linker connecting the repeats of the c-Myb oncoprotein may be due to a positioning function.
    Nucleic acids research, 1996, Oct-15, Volume: 24, Issue:20

    Topics: Acrylamide; Acrylamides; Animals; Binding Sites; Chickens; Chymotrypsin; Conserved Sequence; DNA Probes; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Helix-Turn-Helix Motifs; Models, Molecular; Mutagenesis, Site-Directed; Polydeoxyribonucleotides; Protein Structure, Secondary; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-myb; Repetitive Sequences, Nucleic Acid; Spectrometry, Fluorescence; Trans-Activators; Transcription Factors; Trypsin; Tryptophan

1996
A possible tertiary structure change induced by acrylamide in the DNA-binding domain of the Tn10-encoded Tet repressor. A fluorescence study.
    Journal of protein chemistry, 1996, Volume: 15, Issue:2

    Topics: Acrylamide; Acrylamides; DNA-Binding Proteins; Fluorescence Polarization; Helix-Turn-Helix Motifs; Kinetics; Protein Structure, Tertiary; Repressor Proteins; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

1996
Fluorescence studies on the interaction of a synthetic signal peptide and its analog with liposomes.
    Biochimica et biophysica acta, 1997, Feb-21, Volume: 1324, Issue:1

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Chymotrypsin; Dithionite; Escherichia coli; Liposomes; Membrane Potentials; Molecular Sequence Data; Phosphatidylcholines; Phosphatidylserines; Phosphoenolpyruvate Sugar Phosphotransferase System; Protein Sorting Signals; Sodium Iodide; Spectrometry, Fluorescence; Tryptophan

1997
Time-resolved fluorescence study of a calcium-induced conformational change in prothrombin fragment 1.
    Proteins, 1996, Volume: 24, Issue:4

    Topics: Acrylamide; Acrylamides; Animals; Calcium; Cattle; Peptide Fragments; Protein Precursors; Prothrombin; Spectrometry, Fluorescence; Tryptophan

1996
Immunosuppressor binding to the immunophilin FKBP59 affects the local structural dynamics of a surface beta-strand: time-resolved fluorescence study.
    Biochemistry, 1997, Jun-17, Volume: 36, Issue:24

    Topics: Acrylamide; Acrylamides; Carrier Proteins; DNA-Binding Proteins; Fluorescence Polarization; Heat-Shock Proteins; Immunosuppressive Agents; Models, Molecular; Polyenes; Protein Structure, Secondary; Sirolimus; Spectrometry, Fluorescence; Tacrolimus; Tacrolimus Binding Proteins; Temperature; Thermodynamics; Tryptophan

1997
Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C.
    Biophysical journal, 1997, Volume: 73, Issue:2

    Topics: Acrylamide; Acrylamides; Animals; Calcium; Chickens; Cloning, Molecular; Crystallography, X-Ray; Fluorescence Polarization; Kinetics; Magnesium; Models, Molecular; Muscle Fibers, Fast-Twitch; Muscle, Skeletal; Mutagenesis, Site-Directed; Protein Conformation; Quantum Theory; Recombinant Proteins; Spectrometry, Fluorescence; Time Factors; Troponin C; Tryptophan

1997
Fluorescence spectroscopic studies on interactions between liver annexin VI and nucleotides--a possible role for a tryptophan residue.
    European journal of biochemistry, 1997, Aug-15, Volume: 248, Issue:1

    Topics: Acrylamide; Acrylamides; Adenine Nucleotides; Adenosine Triphosphate; Animals; Annexin A6; Azides; Binding Sites; Energy Metabolism; Humans; In Vitro Techniques; Liver; Nucleotides; Protein Conformation; Spectrometry, Fluorescence; Swine; Tryptophan

1997
Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokiningii S-38: effects of pH, quenching agents, and ligand binding.
    Journal of protein chemistry, 1997, Volume: 16, Issue:7

    Topics: Acrylamide; Acrylamides; Cellulase; Cellulose 1,4-beta-Cellobiosidase; Fluorescence; Hydrogen-Ion Concentration; Kinetics; Ligands; Potassium Iodide; Spectrometry, Fluorescence; Substrate Specificity; Trichoderma; Tryptophan

1997
Modifications induced by insulin-dependent diabetes mellitus on human placental Na+/K+-adenosine triphosphatase.
    The Journal of laboratory and clinical medicine, 1997, Volume: 130, Issue:4

    Topics: Acrylamide; Acrylamides; Adult; Anthracenes; Binding Sites; Diabetes Mellitus, Type 1; Diffusion; Diphenylhexatriene; Enzyme Activation; Female; Fluorescence Polarization; Fluorescent Dyes; Humans; Isothiocyanates; Kinetics; Membrane Fluidity; Microsomes; Ouabain; Placenta; Pregnancy; Pregnancy in Diabetics; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Tryptophan

1997
Mapping the suramin-binding sites of human neutrophil elastase: investigation by fluorescence resonance energy transfer and molecular modeling.
    Biochemistry, 1997, Dec-16, Volume: 36, Issue:50

    Topics: Acrylamide; Acrylamides; Amino Acid Chloromethyl Ketones; Binding Sites; Energy Transfer; Enzyme Inhibitors; Humans; Iodides; Kinetics; Leukocyte Elastase; Models, Molecular; Neutrophils; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry; Suramin; Tryptophan

1997
Functional implications of disulfide bond, Cys45-Cys50, in recombinant prochymosin.
    Biochimica et biophysica acta, 1997, Dec-05, Volume: 1343, Issue:2

    Topics: Acrylamide; Acrylamides; Animals; Caseins; Cattle; Chymosin; Circular Dichroism; Cysteine; Disulfides; Enzyme Activation; Enzyme Precursors; Enzyme Stability; Escherichia coli; Kinetics; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Substrate Specificity; Tryptophan; Urea

1997
Analysis of the conformational stability of the active domain of recombinant mouse TIMP-1 by intrinsic fluorescence.
    Biochemical and biophysical research communications, 1998, Jan-14, Volume: 242, Issue:2

    Topics: Acrylamide; Acrylamides; Animals; Binding Sites; Guanidine; Mice; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tissue Inhibitor of Metalloproteinase-1; Tryptophan

1998
A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 beta-lactamase.
    Biochemistry, 1998, Feb-17, Volume: 37, Issue:7

    Topics: Acrylamide; Acrylamides; Anilino Naphthalenesulfonates; Bacterial Proteins; beta-Lactamases; Circular Dichroism; Escherichia coli; Fluorescence Polarization; Kinetics; Protein Folding; Spectrometry, Fluorescence; Tryptophan

1998
Spectroscopic analysis of halothane binding to the plasma membrane Ca2+-ATPase.
    Biophysical journal, 1998, Volume: 74, Issue:2 Pt 1

    Topics: Acrylamide; Acrylamides; Anesthetics, Inhalation; Binding Sites; Calcium-Transporting ATPases; Ethers; Halothane; Kinetics; Phosphatidylcholines; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Tryptophan; Urea

1998
Steady state and time-resolved fluorescence study of residual structures in an unfolded form of yeast phosphoglycerate kinase.
    Biochemistry, 1998, May-19, Volume: 37, Issue:20

    Topics: Acrylamide; Acrylamides; Cold Temperature; Diffusion; Guanidine; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Phosphoglycerate Kinase; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Solvents; Spectrometry, Fluorescence; Tryptophan; Tyrosine; Viscosity

1998
The orientation of nisin in membranes.
    Biochemistry, 1998, Jun-02, Volume: 37, Issue:22

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Lipid Bilayers; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nisin; Phosphatidylcholines; Phosphatidylglycerols; Spectrometry, Fluorescence; Spin Labels; Tryptophan

1998
Effects of metal binding affinity on the chemical and thermal stability of site-directed mutants of rat oncomodulin.
    Biophysical chemistry, 1998, Apr-20, Volume: 71, Issue:2-3

    Topics: Acrylamide; Acrylamides; Animals; Calcium; Calcium-Binding Proteins; Fluorescence; Guanidine; Hydrogen Bonding; Metals; Mutagenesis, Site-Directed; Mutation; Neoplasm Proteins; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rats; Temperature; Terbium; Thermodynamics; Tryptophan

1998
Effect of single mutations on the structural dynamics of a DNA repair enzyme, the Escherichia coli formamidopyrimidine-DNA glycosylase--a fluorescence study using tryptophan residues as reporter groups.
    European journal of biochemistry, 1998, Apr-15, Volume: 253, Issue:2

    Topics: Acrylamide; Acrylamides; Bacterial Proteins; DNA Ligases; DNA-Formamidopyrimidine Glycosylase; Escherichia coli; Escherichia coli Proteins; N-Glycosyl Hydrolases; Point Mutation; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1998
Time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide.
    Biophysical chemistry, 1998, Jul-13, Volume: 73, Issue:1-2

    Topics: Acrylamide; Acrylamides; Fluorescence; Mathematical Computing; Propylene Glycol; Proteins; Spectrometry, Fluorescence; Time Factors; Tryptophan; Viscosity

1998
Spectroscopic properties and stability of the neurotoxic complex. Vipoxin and its components.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 1998, Volume: 54A, Issue:8

    Topics: Acrylamide; Acrylamides; Drug Stability; Energy Transfer; Enzyme Inhibitors; Guanidine; Kinetics; Models, Molecular; Neurotoxins; Phospholipases A; Phospholipases A2; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Tyrosine; Viper Venoms

1998
Conformational flexibility of domain III of annexin V studied by fluorescence of tryptophan 187 and circular dichroism: the effect of pH.
    Biochemistry, 1998, Aug-25, Volume: 37, Issue:34

    Topics: Acrylamide; Acrylamides; Annexin A5; Circular Dichroism; Fluorescence Polarization; Humans; Hydrogen-Ion Concentration; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Solubility; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Water

1998
Modification of sticholysin II hemolytic activity by free radicals.
    Toxicon : official journal of the International Society on Toxinology, 1998, Volume: 36, Issue:10

    Topics: Acrylamide; Amidines; Animals; Cnidarian Venoms; Erythrocytes; Fluorescence; Free Radicals; Hemolysin Proteins; Humans; Oxidants; Sea Anemones; Sialyltransferases; Tryptophan

1998
Some aspects of beta-lactoglobulin structural properties in solution studied by fluorescence quenching.
    International journal of biological macromolecules, 1998, Volume: 23, Issue:2

    Topics: Acrylamide; Binding Sites; Fluorescence; Kinetics; Lactoglobulins; Palmitic Acid; Protein Conformation; Protein Denaturation; Sodium Nitrite; Solutions; Spectrometry, Fluorescence; Tryptophan; Urea

1998
Fluorescence quenching and time-resolved fluorescence studies on Momordica charantia (bitter gourd) seed lectin.
    Biochemistry and molecular biology international, 1998, Volume: 45, Issue:5

    Topics: Acrylamide; Cesium; Fluorescence; Iodides; Lactose; Lectins; N-Glycosyl Hydrolases; Plant Proteins; Protein Denaturation; Ribosome Inactivating Proteins, Type 2; Spectrometry, Fluorescence; Tryptophan; Urea

1998
Purification and characterization of papaya glutamine cyclotransferase, a plant enzyme highly resistant to chemical, acid and thermal denaturation.
    Biochimica et biophysica acta, 1998, Sep-08, Volume: 1387, Issue:1-2

    Topics: Acrylamide; Aminoacyltransferases; Cysteine Endopeptidases; Glycoproteins; Guanidine; Hydrogen-Ion Concentration; Latex; Plant Proteins; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Temperature; Tryptophan

1998
Conformational changes of the leukocyte NADPH oxidase subunit p47(phox) during activation studied through its intrinsic fluorescence.
    Biochimica et biophysica acta, 1998, Sep-08, Volume: 1387, Issue:1-2

    Topics: Acrylamide; Anions; Binding Sites; Cytochrome b Group; Enzyme Activation; Fatty Acids; Fluorescence; NADPH Oxidases; Neutrophils; Phosphoproteins; Phosphorylation; Protein Conformation; Protein Kinase C; Recombinant Proteins; Sodium Dodecyl Sulfate; Surface-Active Agents; Tryptophan

1998
Tryptophan fluorescence of the lux-specific Vibrio harveyi acyl-ACP thioesterase and its tryptophan mutants: structural properties and ligand-induced conformational change.
    Biochemistry, 1998, Nov-17, Volume: 37, Issue:46

    Topics: Acrylamide; Acyltransferases; Bacterial Proteins; Kinetics; Ligands; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Substrate Specificity; Thiolester Hydrolases; Tryptophan; Tyrosine; Vibrio

1998
Inhibition of myosin ATPase by metal fluoride complexes.
    Biochimica et biophysica acta, 1999, Feb-10, Volume: 1430, Issue:1

    Topics: Acrylamide; Actins; Adenosine Diphosphate; Binding Sites; Circular Dichroism; Enzyme Inhibitors; Fluorescence; Fluorides; Gallium; Magnesium Compounds; Myosins; Tryptophan

1999
Ligand-dependent conformational equilibria of serum albumin revealed by tryptophan fluorescence quenching.
    Biophysical journal, 1999, Volume: 76, Issue:4

    Topics: Acrylamide; Biophysical Phenomena; Biophysics; Chromatography, Gel; Fluorescence Polarization; Humans; In Vitro Techniques; Iodides; Kinetics; Ligands; Oleic Acid; Protein Conformation; Serum Albumin; Spectrometry, Fluorescence; Tryptophan

1999
Resolution and characterization of tryptophyl fluorescence of hen egg-white lysozyme by quenching- and time-resolved spectroscopy.
    Bioscience, biotechnology, and biochemistry, 1999, Volume: 63, Issue:2

    Topics: Acetylglucosamine; Acrylamide; Animals; Chickens; Chromatography, Ion Exchange; Female; Kinetics; Muramidase; Mutagenesis, Site-Directed; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1999
Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I.
    Biochemistry, 1999, Apr-06, Volume: 38, Issue:14

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Animals; Apolipoprotein A-I; Cesium; Chickens; Chlorides; Circular Dichroism; Fatty Acids; Fluorescence Polarization; Fluorescent Dyes; Humans; Lipids; Potassium Iodide; Protein Structure, Secondary; Spectrometry, Fluorescence; Spin Labels; Trifluoroethanol; Tryptophan

1999
Time-resolved distance determination by tryptophan fluorescence quenching: probing intermediates in membrane protein folding.
    Biochemistry, 1999, Apr-20, Volume: 38, Issue:16

    Topics: Acrylamide; Bacterial Outer Membrane Proteins; Biological Transport; Escherichia coli; Fluorescence Polarization; Lipid Bilayers; Normal Distribution; Protein Folding; Spectrometry, Fluorescence; Temperature; Time Factors; Tryptophan

1999
Molecular cloning and expression of adenosine kinase from Leishmania donovani: identification of unconventional P-loop motif.
    The Biochemical journal, 1999, May-01, Volume: 339 ( Pt 3)

    Topics: Acrylamide; Adenosine Kinase; Adenosine Triphosphate; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Consensus Sequence; Escherichia coli; Fluorescence; Humans; Kinetics; Leishmania donovani; Molecular Sequence Data; Molecular Weight; Open Reading Frames; Potassium Iodide; Recombinant Proteins; RNA, Messenger; Sequence Homology, Amino Acid; Trans-Splicing; Tryptophan

1999
The structure and dynamics of partially folded actin.
    Biochemistry, 1999, May-11, Volume: 38, Issue:19

    Topics: Acrylamide; Actins; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Temperature; Tryptophan; Urea

1999
Effect of acrylamide on aldolase structure. I. Induction of intermediate states.
    Biochimica et biophysica acta, 1999, May-18, Volume: 1431, Issue:2

    Topics: Acrylamide; Animals; Binding Sites; Circular Dichroism; Fructose-Bisphosphate Aldolase; Kinetics; Muscles; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Tryptophan

1999
Effect of acrylamide on aldolase structure. II. Characterization of aldolase unfolding intermediates.
    Biochimica et biophysica acta, 1999, May-18, Volume: 1431, Issue:2

    Topics: Acrylamide; Dose-Response Relationship, Drug; Fructose-Bisphosphate Aldolase; Light; Models, Molecular; Protein Conformation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Sulfhydryl Compounds; Tryptophan

1999
Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis.
    The Journal of biological chemistry, 1999, Jun-18, Volume: 274, Issue:25

    Topics: Acrylamide; Adenosine Triphosphate; Affinity Labels; Animals; Antibiotics, Antineoplastic; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; CHO Cells; Cricetinae; Dihydropyridines; Drug Resistance, Multiple; Fluorescence; Ligands; Nucleotides; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Proteolipids; Tryptophan

1999
Tryptophan microstate reshuffling upon the binding of cyclosporin A to human cyclophilin A.
    Proteins, 1999, Jun-01, Volume: 35, Issue:4

    Topics: Acrylamide; Amino Acid Substitution; Base Sequence; Cyclosporine; DNA Primers; Humans; Molecular Sequence Data; Peptidylprolyl Isomerase; Spectrometry, Fluorescence; Tryptophan

1999
Adventures in membrane protein topology. A study of the membrane-bound state of colicin E1.
    The Journal of biological chemistry, 1999, Aug-27, Volume: 274, Issue:35

    Topics: Acrylamide; Amino Acid Sequence; Colicins; Fluorescent Dyes; Ion Channels; Liposomes; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Mutation; Naphthalenes; Peptide Fragments; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan

1999
Optical spectroscopic characterization of single tryptophan mutants of chicken skeletal troponin C: evidence for interdomain interaction.
    Biochemistry, 1999, Sep-14, Volume: 38, Issue:37

    Topics: Acrylamide; Animals; Calcium; Chickens; Circular Dichroism; Muscle, Skeletal; Mutagenesis, Site-Directed; Peptide Fragments; Potassium Iodide; Protein Structure, Secondary; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Temperature; Titrimetry; Troponin C; Tryptophan

1999
The molten globule state of a chimera of human alpha-lactalbumin and equine lysozyme.
    Journal of molecular biology, 1999, Oct-08, Volume: 292, Issue:5

    Topics: Acrylamide; Amino Acid Sequence; Anilino Naphthalenesulfonates; Animals; Circular Dichroism; Enzyme Stability; Fluorescent Dyes; Guanidine; Horses; Humans; Hydrogen-Ion Concentration; Lactalbumin; Molecular Sequence Data; Muramidase; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Recombinant Fusion Proteins; Solvents; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

1999
Effect of self-association on the structural organization of partially folded proteins: inactivated actin.
    Biophysical journal, 1999, Volume: 77, Issue:5

    Topics: Acrylamide; Actins; Anilino Naphthalenesulfonates; Animals; Guanidine; Protein Conformation; Protein Folding; Protein Multimerization; Protein Unfolding; Rabbits; Solvents; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan

1999
Role of the C-terminal helix 9 in the stability and ligandin function of class alpha glutathione transferase A1-1.
    Biochemistry, 1999, Nov-23, Volume: 38, Issue:47

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Binding Sites; Enzyme Stability; Fluorescent Dyes; Glutathione Transferase; Humans; Isoenzymes; Kinetics; Ligands; Mutagenesis, Site-Directed; Peptide Fragments; Phenylalanine; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Deletion; Spectrometry, Fluorescence; Sulfobromophthalein; Tryptophan

1999
Fluorescence and circular dichroism spectroscopic studies on bovine lactoperoxidase.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 1999, Volume: 12, Issue:3

    Topics: Acrylamide; Animals; Cattle; Cesium; Circular Dichroism; Fluorescent Dyes; Guanidine; Iodine; Lactoperoxidase; Milk; Spectrometry, Fluorescence; Tryptophan; Urea

1999
Folding and assembly of dimeric human glutathione transferase A1-1.
    Biochemistry, 1999, Dec-14, Volume: 38, Issue:50

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Binding Sites; Chromatography, High Pressure Liquid; Circular Dichroism; Dimerization; Enzyme Activation; Fluorescent Dyes; Glutathione Transferase; Humans; Isoenzymes; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Stereoisomerism; Thermodynamics; Tryptophan

1999
Structure-function studies of tryptophan mutants of equinatoxin II, a sea anemone pore-forming protein.
    The Biochemical journal, 2000, Feb-15, Volume: 346 Pt 1

    Topics: Acrylamide; Amino Acid Sequence; Animals; Bromosuccinimide; Cattle; Cell Death; Cnidarian Venoms; Cytotoxins; Erythrocytes; Fluorescence; Hemolysis; Liposomes; Molecular Sequence Data; Mutation; Nitrogen; Porins; Protein Structure, Secondary; Recombinant Proteins; Sea Anemones; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Tryptophan; Water

2000
Acrylamide quenching of apo- and holo-alpha-lactalbumin in guanidine hydrochloride.
    Biochemical and biophysical research communications, 2000, Mar-24, Volume: 269, Issue:3

    Topics: Acrylamide; Animals; Apoproteins; Cattle; Guanidine; Kinetics; Lactalbumin; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan

2000
DNA sequence dependent and independent conformational changes in multipartite operator recognition by lambda-repressor.
    Biochemistry, 2000, Mar-28, Volume: 39, Issue:12

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Bacteriophage lambda; Base Sequence; Binding Sites; Circular Dichroism; DNA-Binding Proteins; Fluorescent Dyes; Operator Regions, Genetic; Protein Binding; Protein Conformation; Repressor Proteins; Spectrometry, Fluorescence; Tryptophan; Viral Proteins; Viral Regulatory and Accessory Proteins

2000
Features of F(1)-ATPase catalytic and noncatalytic sites revealed by fluorescence lifetimes and acrylamide quenching of specifically inserted tryptophan residues.
    Biochemistry, 2000, May-09, Volume: 39, Issue:18

    Topics: Acrylamide; Binding Sites; Escherichia coli; Kinetics; Magnesium; Models, Molecular; Mutation; Nucleotides; Protein Binding; Protein Conformation; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan

2000
Lipid binding of the exchangeable apolipoprotein apolipophorin III induces major changes in fluorescence properties of tryptophans 115 and 130.
    Biochemistry, 2000, Jun-13, Volume: 39, Issue:23

    Topics: Acrylamide; Animals; Apolipoproteins; Circular Dichroism; Dimyristoylphosphatidylcholine; Grasshoppers; Guanidine; Insect Proteins; Lipids; Mutation; Nephelometry and Turbidimetry; Protein Binding; Protein Structure, Secondary; Spectrometry, Fluorescence; Trypsin; Tryptophan

2000
Spectroscopic characterization of the interaction between calmodulin-dependent protein kinase I and calmodulin.
    Archives of biochemistry and biophysics, 2000, Jul-01, Volume: 379, Issue:1

    Topics: Acrylamide; Amino Acid Sequence; Binding Sites; Calcium-Calmodulin-Dependent Protein Kinase Type 1; Calcium-Calmodulin-Dependent Protein Kinases; Calmodulin; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Methionine; Molecular Sequence Data; Mutation; Peptide Fragments; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

2000
Isolating and localizing ATP-sensitive tryptophan emission in skeletal myosin subfragment 1.
    Biochemistry, 2000, Sep-26, Volume: 39, Issue:38

    Topics: Acrylamide; Adenosine Triphosphate; Animals; Binding Sites; Models, Chemical; Muscle, Skeletal; Myosin Subfragments; Myosins; Protein Conformation; Quantum Theory; Rabbits; Spectrometry, Fluorescence; Sulfonium Compounds; Tryptophan

2000
Steady state and picosecond time-resolved fluorescence studies on native, desulpho and deflavo xanthine oxidase.
    Biochimica et biophysica acta, 2000, Sep-29, Volume: 1481, Issue:2

    Topics: Acrylamide; Cesium; Chlorides; Potassium Iodide; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Xanthine Oxidase

2000
Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2000, Volume: 56A, Issue:11

    Topics: Acrylamide; Animals; Buffers; Cattle; Circular Dichroism; Humans; Myristic Acid; Protein Structure, Secondary; Quaternary Ammonium Compounds; Serum Albumin; Serum Albumin, Bovine; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Surface-Active Agents; Tromethamine; Tryptophan

2000
Intrinsic fluorescence of the P-glycoprotein multidrug transporter: sensitivity of tryptophan residues to binding of drugs and nucleotides.
    Biochemistry, 2000, Dec-05, Volume: 39, Issue:48

    Topics: Acrylamide; Amino Acid Sequence; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Cricetinae; Iodides; Models, Molecular; Molecular Sequence Data; Nucleotides; Peptides; Pharmaceutical Preparations; Spectrometry, Fluorescence; Tryptophan

2000
Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease.
    Protein science : a publication of the Protein Society, 2000, Volume: 9, Issue:11

    Topics: Acrylamide; Computer Simulation; Escherichia coli; HIV Protease; Kinetics; Models, Molecular; Mutagenesis; Pepstatins; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Time Factors; Tryptophan

2000
Calcium- and magnesium-dependent interactions between the C-terminus of troponin I and the N-terminal, regulatory domain of troponin C.
    Archives of biochemistry and biophysics, 2001, Mar-15, Volume: 387, Issue:2

    Topics: Acrylamide; Amino Acid Substitution; Animals; Binding Sites; Calcium; Iodides; Magnesium; Muscle Contraction; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Rabbits; Sequence Deletion; Spectrometry, Fluorescence; Troponin C; Troponin I; Tryptophan

2001
Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin.
    Biochemical and biophysical research communications, 2001, Jun-01, Volume: 284, Issue:1

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Binding Sites; Cyanogen Bromide; Fluorescent Dyes; Fluorometry; Glucose; Glycation End Products, Advanced; Glycosylation; Humans; Models, Molecular; Peptide Fragments; Peptide Mapping; Serum Albumin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin; Tryptophan

2001
Pseudoreversion of the catalytic activity of Y14F by the additional substitution(s) of tyrosine with phenylalanine in the hydrogen bond network of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
    Biochemistry, 2001, Jun-12, Volume: 40, Issue:23

    Topics: Acrylamide; Amino Acid Substitution; Androstenedione; Catalysis; Crystallography, X-Ray; Deuterium Oxide; Enzyme Activation; Hydrogen Bonding; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Pseudomonas putida; Spectrometry, Fluorescence; Steroid Isomerases; Structure-Activity Relationship; Substrate Specificity; Tryptophan; Tyrosine

2001
On the effect of sodium dodecyl sulfate on the structure of beta-galactosidase from Escherichia coli. A fluorescence study.
    Journal of biochemistry, 2001, Volume: 130, Issue:1

    Topics: Acrylamide; beta-Galactosidase; Escherichia coli; Fluorescence Polarization; Models, Molecular; Protein Structure, Tertiary; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Temperature; Tryptophan

2001
Conformational changes that occur during an RNA-editing adenosine deamination reaction.
    The Journal of biological chemistry, 2001, Oct-12, Volume: 276, Issue:41

    Topics: 2-Aminopurine; Acrylamide; Adenosine Deaminase; Animals; Base Sequence; Binding Sites; DNA Primers; Fluorescence; Hydrolysis; Nucleic Acid Conformation; Rats; RNA Editing; Tryptophan

2001
Cofactor and tryptophan accessibility and unfolding of brain glutamate decarboxylase.
    Archives of biochemistry and biophysics, 2001, Aug-15, Volume: 392, Issue:2

    Topics: Acrylamide; Animals; Anions; Binding Sites; Brain; Cell Line; Cesium; Circular Dichroism; Dimerization; Dose-Response Relationship, Drug; Glutamate Decarboxylase; Guanidine; Insecta; Iodine; Ions; Kinetics; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Spectrometry, Fluorescence; Tryptophan

2001
Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes.
    Biochemistry, 2001, Aug-21, Volume: 40, Issue:33

    Topics: Acrylamide; Amino Acid Sequence; Apoptosis; bcl-2-Associated X Protein; Cell Membrane; Diphenylhexatriene; Gene Deletion; Kinetics; Liposomes; Mitochondria; Molecular Sequence Data; Mutation; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-bcl-2; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Infrared; Tryptophan

2001
Probing the structural diversities of long alpha-neurotoxins by fluorescence quenching studies.
    Journal of protein chemistry, 2001, Volume: 20, Issue:2

    Topics: Acrylamide; Animals; Bungarus; Colubridae; Computer Simulation; Fluorescence; Iodides; Models, Molecular; Neurotoxins; Protein Conformation; Snake Venoms; Structure-Activity Relationship; Tryptophan

2001
Role of conformational changes in the heme-dependent regulation of human soluble guanylate cyclase.
    Journal of inorganic biochemistry, 2001, Dec-15, Volume: 87, Issue:4

    Topics: Acrylamide; Circular Dichroism; Enzyme Activation; Guanylate Cyclase; Heme; Humans; Indazoles; Models, Chemical; Models, Molecular; Nitric Oxide; Nitric Oxide Donors; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan

2001
Binding of prion protein to lipid membranes and implications for prion conversion.
    Journal of molecular biology, 2002, Feb-01, Volume: 315, Issue:5

    Topics: 1,2-Dipalmitoylphosphatidylcholine; Acrylamide; Animals; Cholesterol; Circular Dichroism; Cricetinae; Fluoresceins; Fluorescence; Fourier Analysis; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Kinetics; Lipid Bilayers; Liposomes; Membrane Microdomains; Mesocricetus; Models, Molecular; Phosphatidylglycerols; Prions; Protein Binding; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Sphingomyelins; Static Electricity; Tryptophan

2002
Second derivative fluorescence spectra of indole compounds.
    Journal of biochemistry, 2002, Volume: 131, Issue:3

    Topics: Acrylamide; Protein Conformation; Protein Denaturation; Protein Folding; Proteins; Spectrometry, Fluorescence; Spectrum Analysis; Tryptophan; Tyrosine

2002
Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
    Physiological chemistry and physics and medical NMR, 2001, Volume: 33, Issue:2

    Topics: Acrylamide; Animals; Brain; Dose-Response Relationship, Drug; Goats; Guanosine Triphosphate; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Nucleotides; Protein Binding; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Time Factors; Tryptophan; Tubulin; Urea

2001
Effect of heavy water on protein flexibility.
    Biophysical journal, 2002, Volume: 82, Issue:6

    Topics: Acrylamide; Animals; Biophysical Phenomena; Biophysics; Deuterium Oxide; In Vitro Techniques; Kinetics; Luminescence; Protein Conformation; Protein Folding; Proteins; Thermodynamics; Tryptophan

2002
Half-of-the-sites reactivity of F235C lambda-repressor: implications for the structure of the whole repressor.
    Protein engineering, 2002, Volume: 15, Issue:5

    Topics: Acrylamide; Circular Dichroism; Cysteine; DNA-Binding Proteins; Fluorescent Dyes; Mutagenesis, Site-Directed; Protein Denaturation; Protein Structure, Tertiary; Repressor Proteins; Spectrometry, Fluorescence; Sulfhydryl Compounds; Tryptophan; Urea; Viral Proteins; Viral Regulatory and Accessory Proteins

2002
Unfolding and conformational studies on bovine adrenodoxin probed by engineered intrinsic tryptophan fluorescence.
    Biochemistry, 2002, Sep-10, Volume: 41, Issue:36

    Topics: Acrylamide; Adrenodoxin; Amino Acid Substitution; Animals; Cattle; Energy Transfer; Hot Temperature; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

2002
Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin.
    Biochemistry, 2002, Oct-08, Volume: 41, Issue:40

    Topics: Acrylamide; Bacteria; Lipid Metabolism; Nisin; Spectrometry, Fluorescence; Spin Labels; Tryptophan; Uridine Diphosphate N-Acetylmuramic Acid

2002
Fluorescence quenching of dimeric and monomeric forms of yeast hexokinase (PII): effect of substrate binding steady-state and time-resolved fluorescence studies.
    Physiological chemistry and physics and medical NMR, 2002, Volume: 34, Issue:1

    Topics: Acrylamide; Crystallography; Dimerization; Enzyme Activation; Glucose; Hexokinase; Isoenzymes; Macromolecular Substances; Molecular Conformation; Potassium Iodide; Spectrometry, Fluorescence; Substrate Specificity; Tryptophan; Yeasts

2002
Differences in nucleotide-binding site of isoapyrases deduced from tryptophan fluorescence.
    Phytochemistry, 2003, Volume: 63, Issue:1

    Topics: Acrylamide; Adenosine Diphosphate; Adenosine Triphosphate; Apyrase; Binding Sites; Cesium; Iodides; Isoenzymes; Kinetics; Nucleotides; Photobleaching; Solanum tuberosum; Spectrometry, Fluorescence; Substrate Specificity; Tryptophan

2003
Inter-subunit recognition and manifestation of segmental mobility in Escherichia coli RNA polymerase: a case study with omega-beta' interaction.
    Biophysical chemistry, 2003, Mar-25, Volume: 103, Issue:3

    Topics: Acrylamide; Amino Acid Sequence; Cysteine; DNA-Directed RNA Polymerases; Escherichia coli; Fluorescence Polarization; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Protein Denaturation; Protein Folding; Protein Renaturation; Protein Structure, Secondary; Protein Subunits; Spectrometry, Fluorescence; Thermus; Tryptophan

2003
Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability.
    The Journal of biological chemistry, 2003, Sep-26, Volume: 278, Issue:39

    Topics: Acrylamide; Binding Sites; Circular Dichroism; Cysteine Synthase; Enzyme Stability; Fluorescence; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Structure-Activity Relationship; Tryptophan

2003
Examination of EmrE conformational differences in various membrane mimetic environments.
    Biochemistry and cell biology = Biochimie et biologie cellulaire, 2003, Volume: 81, Issue:2

    Topics: Acrylamide; Amino Acid Sequence; Antiporters; Cell Membrane; Circular Dichroism; Drug Resistance, Multiple, Bacterial; Escherichia coli; Escherichia coli Proteins; Fluorescence Polarization; Humans; Membrane Proteins; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Sodium Dodecyl Sulfate; Solubility; Spectrometry, Fluorescence; Tryptophan

2003
The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.
    Biophysical journal, 2003, Volume: 85, Issue:3

    Topics: Acrylamide; Algorithms; Biophysics; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electrons; Fluorescence; Hydrogen; Kinetics; Models, Statistical; Molecular Conformation; Mutation; Protein Conformation; Spectrometry, Fluorescence; Time Factors; Trichosanthes; Tryptophan

2003
Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core.
    The Journal of biological chemistry, 2003, Nov-28, Volume: 278, Issue:48

    Topics: Acrylamide; Dimerization; Escherichia coli; Glycerol; Kinetics; Luminescent Measurements; Models, Molecular; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Rhodospirillum rubrum; Spectrometry, Fluorescence; Spectrophotometry; Temperature; Time Factors; Tryptophan

2003
C-terminal functional unit of Rapana thomasiana (marine snail, gastropod) hemocyanin isoform RtH1: isolation and characterization.
    Biochimica et biophysica acta, 2003, Sep-23, Volume: 1651, Issue:1-2

    Topics: Acrylamide; Amino Acids; Animals; Hemocyanins; Hydrogen-Ion Concentration; Peptide Fragments; Protein Conformation; Protein Isoforms; Protein Subunits; Seawater; Snails; Temperature; Tryptophan; Tyrosine

2003
The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-alpha-helical bundle domain.
    European journal of biochemistry, 2003, Volume: 270, Issue:19

    Topics: Acrylamide; Cesium; Imaging, Three-Dimensional; Iodides; Models, Molecular; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spectrum Analysis; Structural Homology, Protein; Tryptophan

2003
A study of tryptophan fluorescence quenching of bifunctional alginate lyase from a marine bacterium Pseudoalteromonas sp. strain No. 272 by acrylamide.
    Bioscience, biotechnology, and biochemistry, 2003, Volume: 67, Issue:9

    Topics: Acrylamide; Methylation; Oligosaccharides; Polysaccharide-Lyases; Pseudoalteromonas; Spectrometry, Fluorescence; Substrate Specificity; Tryptophan

2003
Steady-state kinetics and tryptophan fluorescence properties of halohydrin dehalogenase from Agrobacterium radiobacter. Roles of W139 and W249 in the active site and halide-induced conformational change.
    Biochemistry, 2003, Dec-02, Volume: 42, Issue:47

    Topics: Acrylamide; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Bromides; Catalysis; Hydrogen-Ion Concentration; Hydrolases; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Protein Binding; Protein Conformation; Rhizobium; Spectrometry, Fluorescence; Stereoisomerism; Substrate Specificity; Tryptophan

2003
Increase in molecular rigidity of the protein conformation of brain Na+-K+-ATPase by modification with 4-hydroxy-2-nonenal.
    Biological & pharmaceutical bulletin, 2003, Volume: 26, Issue:12

    Topics: Acrylamide; Aldehydes; Animals; Anisotropy; Brain; Dose-Response Relationship, Drug; Ethylmaleimide; Fluorescence; Guanidine; Lipid Peroxidation; Molecular Conformation; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Sulfhydryl Compounds; Swine; Tryptophan

2003
Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain.
    Biopolymers, 2003, Volume: 70, Issue:4

    Topics: Acrylamide; Amino Acid Substitution; Animals; Apoproteins; Horses; Iodides; Myoglobin; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Whales

2003
Hypochlorite action on plasma fibronectin promotes its extended conformation in complexes with antibodies.
    Journal of protein chemistry, 2003, Volume: 22, Issue:5

    Topics: Acrylamide; Antibodies; Antigen-Antibody Complex; Chlorine; Enzyme-Linked Immunosorbent Assay; Fibronectins; Fluorescence; Humans; Hypochlorous Acid; Luminescent Measurements; Tryptophan; Tyrosine

2003
Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate.
    Biochemistry, 2004, Jan-13, Volume: 43, Issue:1

    Topics: Acrylamide; Bacillus thuringiensis; Bacillus thuringiensis Toxins; Bacterial Proteins; Bacterial Toxins; Endotoxins; Hemolysin Proteins; Ion Channels; Lipid Bilayers; Liposomes; Membrane Proteins; Phosphatidylcholines; Phospholipids; Solutions; Spectrometry, Fluorescence; Tryptophan; Water

2004
Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity.
    Biochemical and biophysical research communications, 2004, Feb-06, Volume: 314, Issue:2

    Topics: Acrylamide; Biochemistry; Circular Dichroism; Dose-Response Relationship, Drug; Escherichia coli; Kinetics; Lipids; Peptide Biosynthesis; Peptides; Proline; Spectrometry, Fluorescence; Tryptophan

2004
Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5.
    The Journal of biological chemistry, 2004, Apr-09, Volume: 279, Issue:15

    Topics: Acrylamide; Amino Acid Sequence; Amino Acids; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Bacteria; Binding Sites; Circular Dichroism; Dose-Response Relationship, Drug; Drug Design; Erythrocytes; Hemolysis; Humans; Kinetics; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Molecular Sequence Data; Peptides; Protein Conformation; Protein Engineering; Protein Precursors; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Spectrophotometry; Time Factors; Tryptophan

2004
Effects of cavity-forming mutations on the internal dynamics of azurin.
    Biophysical journal, 2004, Volume: 86, Issue:2

    Topics: Acrylamide; Amino Acid Substitution; Azurin; Mutation; Porosity; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Structure-Activity Relationship; Temperature; Tryptophan

2004
Conformational changes of beta-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles. A fluorescence and CD study.
    European journal of biochemistry, 2004, Volume: 271, Issue:4

    Topics: Acrylamide; Animals; Cattle; Circular Dichroism; Dioctyl Sulfosuccinic Acid; Kinetics; Lactoglobulins; Micelles; Models, Molecular; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Water

2004
Insight into the activation mechanism of Bordetella pertussis adenylate cyclase by calmodulin using fluorescence spectroscopy.
    European journal of biochemistry, 2004, Volume: 271, Issue:4

    Topics: 2-Naphthylamine; Acrylamide; Adenosine Triphosphate; Adenylyl Cyclases; Amino Acid Substitution; Bordetella pertussis; Calmodulin; Catalytic Domain; Entropy; Enzyme Activation; Fluorescence Polarization; Kinetics; Models, Chemical; Molecular Weight; ortho-Aminobenzoates; Protein Binding; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

2004
Role of hydration in the conformational transitions between unliganded and liganded forms of loop 13 of the Na+/glucose cotransporter 1.
    Biochemical and biophysical research communications, 2004, Mar-19, Volume: 315, Issue:4

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Circular Dichroism; Glycerol; Hydrophobic and Hydrophilic Interactions; Kinetics; Ligands; Membrane Glycoproteins; Monosaccharide Transport Proteins; Phlorhizin; Protein Binding; Protein Conformation; Protein Denaturation; Sodium-Glucose Transporter 1; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Urea; Water

2004
Membrane binding and translocation of cell-penetrating peptides.
    Biochemistry, 2004, Mar-30, Volume: 43, Issue:12

    Topics: Acrylamide; Amino Acid Sequence; Bromine; Carrier Proteins; Cell Membrane Permeability; Cell-Penetrating Peptides; Coumarins; Fluorescence Resonance Energy Transfer; Gene Products, tat; Lipid Bilayers; Lysophospholipids; Membrane Microdomains; Molecular Sequence Data; Oligonucleotides; Peptides; Phosphatidylcholines; Phosphatidylglycerols; Protein Binding; Protein Conformation; Protein Transport; Spectrometry, Fluorescence; Tryptophan

2004
HIV Rev self-assembly is linked to a molten-globule to compact structural transition.
    Biophysical chemistry, 2004, Mar-01, Volume: 108, Issue:1-3

    Topics: Acrylamide; Binding Sites; Circular Dichroism; Cloning, Molecular; Escherichia coli; Gene Products, rev; HIV-1; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Protein Denaturation; Protein Folding; rev Gene Products, Human Immunodeficiency Virus; Sodium Chloride; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

2004
Molten globule-like folding intermediate of asialofetuin at acidic pH.
    Biochimica et biophysica acta, 2004, Jun-01, Volume: 1699, Issue:1-2

    Topics: Acids; Acrylamide; alpha-Fetoproteins; Animals; Asialoglycoproteins; Cattle; Circular Dichroism; Fetuins; Glycosylation; Hydrogen-Ion Concentration; Protein Conformation; Protein Folding; Spectrometry, Fluorescence; Temperature; Tryptophan

2004
Tryptophan fluorescence monitors structural changes accompanying signalling state formation in the photocycle of photoactive yellow protein.
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2004, Volume: 3, Issue:6

    Topics: Acrylamide; Bacterial Proteins; Cloning, Molecular; Darkness; Escherichia coli; Halorhodospira halophila; Kinetics; Light; Luminescent Proteins; Recombinant Proteins; Signal Transduction; Spectrometry, Fluorescence; Tryptophan

2004
C-terminus loop 13 of Na+ glucose cotransporter SGLT1 contains a binding site for alkyl glucosides.
    Biochemistry, 2004, Aug-31, Volume: 43, Issue:34

    Topics: Acrylamide; Amino Acid Sequence; Binding Sites; Binding, Competitive; Glucose; Glucosides; Hexanols; Ligands; Membrane Glycoproteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Peptide Fragments; Photoaffinity Labels; Protein Structure, Secondary; Sodium; Sodium-Glucose Transporter 1; Spectrometry, Fluorescence; Stereoisomerism; Tryptophan

2004
Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocols.
    Biophysical journal, 2004, Volume: 87, Issue:3

    Topics: Acrylamide; Azurin; Biophysical Phenomena; Biophysics; Copper; Gadolinium; Guanidine; Hot Temperature; Ligands; Phase Transition; Protein Conformation; Protein Folding; Pseudomonas aeruginosa; Spectrometry, Fluorescence; Temperature; Thermodynamics; Time Factors; Tryptophan

2004
Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size.
    Biochemistry, 2004, Sep-21, Volume: 43, Issue:37

    Topics: Acrylamide; Amino Acid Sequence; Animals; Apolipoprotein A-I; Humans; Lipoproteins, HDL; Models, Molecular; Molecular Sequence Data; Mutation; Particle Size; Protein Conformation; Spin Labels; Tryptophan

2004
Proton motive force mediates a reorientation of the cytosolic domains of the multidrug transporter LmrP.
    Cellular and molecular life sciences : CMLS, 2004, Volume: 61, Issue:19-20

    Topics: Acrylamide; Aspartic Acid; Bacterial Proteins; Benzimidazoles; Biological Transport; Cell Membrane; Cytosol; Dose-Response Relationship, Drug; Drug Resistance, Multiple; Hydrogen-Ion Concentration; Lactococcus lactis; Ligands; Liposomes; Membrane Transport Proteins; Protein Binding; Protein Structure, Tertiary; Proteolipids; Protons; Sepharose; Spectroscopy, Fourier Transform Infrared; Tetracycline; Time Factors; Tryptophan

2004
Comparative studies on the structure and stability of fluorescent proteins EGFP, zFP506, mRFP1, "dimer2", and DsRed1.
    Biochemistry, 2004, Nov-30, Volume: 43, Issue:47

    Topics: Acrylamide; Amino Acid Sequence; Circular Dichroism; Dose-Response Relationship, Drug; Escherichia coli; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Gadolinium; Green Fluorescent Proteins; Kinetics; Luminescent Proteins; Molecular Sequence Data; Plasmids; Protein Binding; Protein Conformation; Protein Denaturation; Protein Structure, Quaternary; Recombinant Proteins; Red Fluorescent Protein; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Tryptophan; Ultraviolet Rays

2004
Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence.
    The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9

    Topics: Acetylcholine; Acrylamide; Animals; Binding Sites; Carrier Proteins; Crystallography, X-Ray; Humans; Ligands; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Snails; Spectrometry, Fluorescence; Time Factors; Tryptophan

2005
Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana Harms. ex Diels. lectin.
    Acta biochimica et biophysica Sinica, 2005, Volume: 37, Issue:1

    Topics: Acrylamide; Amino Acids; Arginine; Binding Sites; Carbohydrates; Circular Dichroism; Hemagglutination; Mannose; Millettia; Oligosaccharides; Oxygen; Plant Lectins; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan; Ultraviolet Rays

2005
Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide.
    The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17

    Topics: Acrylamide; Amino Acid Motifs; Anti-Infective Agents; Antimicrobial Cationic Peptides; Cell Differentiation; Dose-Response Relationship, Drug; Endotoxins; Humans; Lactoferrin; Lipopolysaccharides; Magnetic Resonance Spectroscopy; Micelles; Models, Chemical; Models, Molecular; Peptides; Phosphates; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Static Electricity; Teichoic Acids; Tryptophan

2005
TBADH activity in water-miscible organic solvents: correlations between enzyme performance, enantioselectivity and protein structure through spectroscopic studies.
    Organic & biomolecular chemistry, 2005, Mar-07, Volume: 3, Issue:5

    Topics: Acetonitriles; Acrylamide; Alcohol Dehydrogenase; Circular Dichroism; Ethanol; Methanol; Oxidation-Reduction; Pentanones; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Subunits; Spectrometry, Fluorescence; Stereoisomerism; Thermoanaerobacter; Tryptophan; Water

2005
Dimeric transthyretin variant assembles into spherical neurotoxins.
    Biochemistry, 2005, Mar-08, Volume: 44, Issue:9

    Topics: Acrylamide; Amino Acid Substitution; Anilino Naphthalenesulfonates; Cell Death; Cell Line, Tumor; Chromatography, Gel; Dimerization; Genetic Variation; Humans; Isoleucine; Microscopy, Atomic Force; Nephelometry and Turbidimetry; Neuroblastoma; Neurotoxins; Prealbumin; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

2005
The characterization of plasma membrane Ca2+-ATPase in rich sphingomyelin-cholesterol domains.
    FEBS letters, 2005, Apr-25, Volume: 579, Issue:11

    Topics: Acrylamide; Calcium-Transporting ATPases; Cell Membrane; Cholesterol; Fluorescence; Phase Transition; Phosphatidylcholines; Proteolipids; Spectrometry, Fluorescence; Sphingomyelins; Tryptophan

2005
Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy.
    Biochemistry, 2005, May-03, Volume: 44, Issue:17

    Topics: Acrylamide; Adenosine Triphosphatases; Amino Acid Substitution; Bacterial Proteins; Escherichia coli Proteins; Genetic Complementation Test; Membrane Proteins; Membrane Transport Proteins; Protein Binding; Protein Conformation; Protein Transport; SEC Translocation Channels; SecA Proteins; Solubility; Spectrometry, Fluorescence; Temperature; Tryptophan

2005
Structural rearrangements in the active site of smooth-muscle myosin.
    Biophysical journal, 2005, Volume: 89, Issue:3

    Topics: Acrylamide; Actins; Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Binding Sites; Cell Line; Chickens; Crystallography, X-Ray; Dictyostelium; DNA, Complementary; Dose-Response Relationship, Drug; Fluorescence Resonance Energy Transfer; Hydrolysis; Insecta; Kinetics; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Myosin Type II; Myosins; Nucleotides; Protein Conformation; Protein Structure, Tertiary; Temperature; Time Factors; Tryptophan

2005
Nucleotides regulate the conformational state of the small terminase subunit from bacteriophage lambda: implications for the assembly of a viral genome-packaging motor.
    Biochemistry, 2005, Jul-19, Volume: 44, Issue:28

    Topics: Acrylamide; Adenosine Diphosphate; Adenosine Triphosphate; Azides; Bacteriophage lambda; Binding, Competitive; Dimerization; DNA-Binding Proteins; DNA, Viral; Endodeoxyribonucleases; Genome, Viral; Molecular Motor Proteins; Photoaffinity Labels; Protein Binding; Protein Conformation; Protein Subunits; Sequence Deletion; Spectrometry, Fluorescence; Tryptophan; Viral Proteins; Virus Assembly

2005
Effect of structural transition of the host assembly on dynamics of an ion channel peptide: a fluorescence approach.
    Biophysical journal, 2005, Volume: 89, Issue:5

    Topics: Acrylamide; Bacillus; Circular Dichroism; Dose-Response Relationship, Drug; Gramicidin; Ion Channels; Ions; Kinetics; Micelles; Models, Statistical; Protein Conformation; Sodium Dodecyl Sulfate; Solvents; Spectrometry, Fluorescence; Spectrophotometry; Spectrum Analysis, Raman; Time Factors; Tryptophan; Ultraviolet Rays; Water

2005
Conformational dynamics of estrogen receptors alpha and beta as revealed by intrinsic tryptophan fluorescence and circular dichroism.
    Journal of molecular endocrinology, 2005, Volume: 35, Issue:2

    Topics: Acrylamide; Circular Dichroism; Estradiol; Estrogen Receptor alpha; Estrogen Receptor beta; Female; Humans; Male; Microscopy, Atomic Force; Particle Size; Protein Conformation; Protein Denaturation; Protein Folding; Protein Isoforms; Recombinant Proteins; Tryptophan

2005
Membrane-bound peptides mimicking transmembrane Vph1p helix 7 of yeast V-ATPase: a spectroscopic and polarity mismatch study.
    Biochimica et biophysica acta, 2005, Oct-15, Volume: 1716, Issue:2

    Topics: Acrylamide; Amino Acid Sequence; Amino Acids; Arginine; Cell Membrane; Circular Dichroism; Electron Spin Resonance Spectroscopy; Histidine; Lipid Bilayers; Lipids; Models, Statistical; Molecular Sequence Data; Mutation; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan; Vacuolar Proton-Translocating ATPases

2005
Anomalous "unquenching" of the fluorescence decay times of beta-lactoglobulin induced by the known quencher acrylamide.
    Journal of photochemistry and photobiology. B, Biology, 2006, Feb-01, Volume: 82, Issue:2

    Topics: Acrylamide; Fluorescence; Hydrogen-Ion Concentration; Lactoglobulins; Models, Molecular; Molecular Structure; Time Factors; Tryptophan

2006
Low versus high molecular weight poly(ethylene glycol)-induced states of stem bromelain at low pH: stabilization of molten globule and unfolded states.
    Biopolymers, 2006, Apr-05, Volume: 81, Issue:5

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Biopolymers; Bromelains; Circular Dichroism; Enzyme Stability; Ethylene Glycol; Guanidine; Hydrogen-Ion Concentration; Molecular Conformation; Molecular Weight; Polyethylene Glycols; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan

2006
Steady-state fluorescence quenching applications for studying protein structure and dynamics.
    Journal of photochemistry and photobiology. B, Biology, 2006, Jun-01, Volume: 83, Issue:3

    Topics: Acrylamide; Algorithms; Cesium; Chlorides; Energy Transfer; Fluorescence; Fluorescence Resonance Energy Transfer; Protein Conformation; Proteins; Temperature; Tryptophan

2006
Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence.
    Biochemistry, 2006, Feb-28, Volume: 45, Issue:8

    Topics: Acrylamide; alpha-Synuclein; Amino Acid Substitution; Amyloid; Anilino Naphthalenesulfonates; Fluorescence; Fluorescence Polarization; Fluorescence Resonance Energy Transfer; Protein Structure, Secondary; Solvents; Time Factors; Tryptophan; Tyrosine

2006
Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling.
    Biophysical journal, 2006, Aug-01, Volume: 91, Issue:3

    Topics: Acrylamide; Bacillus; Biophysics; Kinetics; Models, Molecular; Models, Statistical; Mutation; Solvents; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan; X-Rays

2006
A carboxyl-terminal hydrophobic interface is critical to sodium channel function. Relevance to inherited disorders.
    The Journal of biological chemistry, 2006, Aug-18, Volume: 281, Issue:33

    Topics: Acrylamide; Amino Acid Sequence; Amino Acid Substitution; Arrhythmias, Cardiac; Cell Line; Computational Biology; EF Hand Motifs; Humans; Hydrophobic and Hydrophilic Interactions; Ion Channel Gating; Molecular Sequence Data; Muscle Proteins; NAV1.5 Voltage-Gated Sodium Channel; Peptide Fragments; Protein Structure, Secondary; Protein Subunits; Sodium Channels; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

2006
Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter.
    The Biochemical journal, 2006, Oct-15, Volume: 399, Issue:2

    Topics: Acrylamide; Adenosine Diphosphate; Adenosine Triphosphate; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Cesium; CHO Cells; Cricetinae; Cricetulus; Fluorescence; Iodine; Kinetics; Multidrug Resistance-Associated Proteins; Protein Conformation; Trinitrobenzenes; Tryptophan

2006
Effects of guanidine hydrochloride on the conformation and enzyme activity of streptomycin adenylyltransferase monitored by circular dichroism and fluorescence spectroscopy.
    Biochemistry. Biokhimiia, 2006, Volume: 71, Issue:11

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Circular Dichroism; Guanidine; Mycobacterium tuberculosis; Nucleotidyltransferases; Potassium Iodide; Protein Binding; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan

2006
Modulation of gramicidin channel conformation and organization by hydrophobic mismatch in saturated phosphatidylcholine bilayers.
    Biochimica et biophysica acta, 2007, Volume: 1768, Issue:5

    Topics: Acrylamide; Centrifugation, Density Gradient; Circular Dichroism; Gramicidin; Hydrophobic and Hydrophilic Interactions; Ion Channels; Lipid Bilayers; Phosphatidylcholines; Protein Structure, Quaternary; Spectrometry, Fluorescence; Time Factors; Tryptophan

2007
The role of cofactor binding in tryptophan accessibility and conformational stability of His-tagged D-amino acid oxidase from Trigonopsis variabilis.
    Biochimica et biophysica acta, 2007, Volume: 1774, Issue:5

    Topics: Acrylamide; Amino Acid Sequence; D-Amino-Acid Oxidase; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Denaturation; Spectrophotometry, Ultraviolet; Tryptophan; Yeasts

2007
Effect of structural transition of the host assembly on dynamics of a membrane-bound tryptophan analogue.
    Biophysical chemistry, 2007, Volume: 129, Issue:2-3

    Topics: Acrylamide; Anisotropy; Cell Membrane; Membrane Proteins; Micelles; Models, Chemical; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Tryptophan

2007
Fluorescence quenching and time-resolved fluorescence studies of alpha-mannosidase from Aspergillus fischeri (NCIM 508).
    Journal of fluorescence, 2007, Volume: 17, Issue:6

    Topics: Acrylamide; alpha-Mannosidase; Aspergillus; Bromosuccinimide; Cesium; Chlorides; Potassium Iodide; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Succinimides; Tryptophan

2007
Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.
    Biophysical journal, 2008, Mar-15, Volume: 94, Issue:6

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Disulfides; Fluorescence; Iodides; Molecular Conformation; Molecular Sequence Data; Peptides; Proteins; Ribonucleases; Spectrometry, Fluorescence; Time Factors; Tryptophan; Urea

2008
Membrane-bound peptides from V-ATPase subunit a do not interact with an indole-type inhibitor.
    Journal of peptide science : an official publication of the European Peptide Society, 2008, Volume: 14, Issue:4

    Topics: Acrylamide; Amino Acid Sequence; Amino Acids; Arginine; Fluorescence Resonance Energy Transfer; Indoles; Lipid Bilayers; Lipids; Membrane Proteins; Molecular Sequence Data; Peptides; Phosphatidylcholines; Phosphatidylglycerols; Piperidines; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan; Vacuolar Proton-Translocating ATPases

2008
Binding of LL-37 to model biomembranes: insight into target vs host cell recognition.
    Biochimica et biophysica acta, 2008, Volume: 1778, Issue:4

    Topics: Acrylamide; Amyloid; Antimicrobial Cationic Peptides; Cathelicidins; Circular Dichroism; Fluorescence Resonance Energy Transfer; Humans; Kinetics; Lipid Bilayers; Liposomes; Microbial Sensitivity Tests; Phosphatidylcholines; Protein Binding; Protein Structure, Secondary; Spectrometry, Fluorescence; Time Factors; Tryptophan

2008
Molecularly imprinted polymer prepared with bonded beta-cyclodextrin and acrylamide on functionalized silica gel for selective recognition of tryptophan in aqueous media.
    Journal of chromatography. A, 2008, Apr-11, Volume: 1187, Issue:1-2

    Topics: Acrylamide; Adsorption; beta-Cyclodextrins; Chromatography, High Pressure Liquid; Molecular Imprinting; Silica Gel; Silicon Dioxide; Stereoisomerism; Tryptophan

2008
The secondary structure of calcineurin regulatory region and conformational change induced by calcium/calmodulin binding.
    The Journal of biological chemistry, 2008, Apr-25, Volume: 283, Issue:17

    Topics: Acrylamide; Calcineurin; Calcium; Calmodulin; Catalytic Domain; Humans; Models, Biological; Molecular Conformation; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared; Tryptophan

2008
Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.
    The Journal of biological chemistry, 2008, Oct-31, Volume: 283, Issue:44

    Topics: Acrylamide; Amino Acid Sequence; Amino Acids; Circular Dichroism; Gene Expression Regulation, Viral; Kinetics; Magnetic Resonance Spectroscopy; Models, Biological; Molecular Sequence Data; Mutation; Peptide Hydrolases; Protein Structure, Secondary; Tryptophan; Viral Envelope Proteins

2008
Benzodiazepine-mediated structural changes in the multidrug transporter P-glycoprotein: an intrinsic fluorescence quenching analysis.
    The Journal of membrane biology, 2008, Volume: 223, Issue:3

    Topics: Acrylamide; Adenosine Triphosphate; Animals; Anti-Anxiety Agents; ATP Binding Cassette Transporter, Subfamily B; Benzodiazepines; Flurazepam; Iodides; Mice; Micelles; Pichia; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

2008
No effect of covalently linked poly(ethylene glycol) chains on protein internal dynamics.
    Biochimica et biophysica acta, 2009, Volume: 1794, Issue:3

    Topics: Acrylamide; Azurin; Enzyme Stability; Luminescent Measurements; Oxygen; Polyethylene Glycols; Protein Conformation; Protein Folding; Proteins; Ribonuclease T1; Spectrometry, Fluorescence; Tryptophan

2009
Equilibrium unfolding of the retinoid X receptor ligand binding domain and characterization of an unfolding intermediate.
    Biophysical chemistry, 2009, Volume: 141, Issue:1

    Topics: Acrylamide; Alitretinoin; Circular Dichroism; Dose-Response Relationship, Drug; Fluorescein; Fluorescent Dyes; Humans; Ligands; Nitrates; Protein Denaturation; Protein Folding; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary; Retinoid X Receptors; Thermodynamics; Tretinoin; Tryptophan; Ultracentrifugation

2009
Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt.
    The Journal of biological chemistry, 2009, May-22, Volume: 284, Issue:21

    Topics: Acrylamide; Colipases; Humans; Kinetics; Lactones; Lipase; Mutant Proteins; Orlistat; Protein Conformation; Spectrometry, Fluorescence; Structure-Activity Relationship; Taurodeoxycholic Acid; Time Factors; Tryptophan

2009
Light-induced aggregation of type I soluble tumor necrosis factor receptor.
    Journal of pharmaceutical sciences, 2009, Volume: 98, Issue:9

    Topics: Acrylamide; Excipients; Oxidation-Reduction; Protein Conformation; Protein Stability; Receptors, Tumor Necrosis Factor, Type I; Sodium Azide; Sulfhydryl Compounds; Tryptophan; Ultraviolet Rays

2009
Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: evidence of gated quencher penetration.
    Biochemistry, 2009, Aug-11, Volume: 48, Issue:31

    Topics: Acrylamide; Alcohol Dehydrogenase; Animals; Crystallography, X-Ray; Diffusion; Dose-Response Relationship, Drug; Horses; Liver; Luminescent Measurements; Models, Chemical; Solutions; Temperature; Tryptophan

2009
Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K(+) channels.
    Biochimica et biophysica acta, 2009, Volume: 1788, Issue:9

    Topics: Acrylamide; Biophysical Phenomena; Circular Dichroism; Desulfurococcaceae; Dimyristoylphosphatidylcholine; Humans; Ion Channel Gating; Large-Conductance Calcium-Activated Potassium Channels; Lipid Bilayers; Micelles; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phospholipid Ethers; Potassium Channels; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan

2009
Tryptophan exposure and accessibility in the chitooligosaccharide-specific phloem exudate lectin from pumpkin (Cucurbita maxima). A fluorescence study.
    Journal of photochemistry and photobiology. B, Biology, 2009, Oct-06, Volume: 97, Issue:1

    Topics: Acrylamide; Cucurbita; Fluorescence; Ligands; Oligosaccharides; Plant Lectins; Protein Denaturation; Spectrometry, Fluorescence; Tryptophan

2009
Different modes of antibiotic action of homodimeric and monomeric bactenecin, a cathelicidin-derived antibacterial peptide.
    BMB reports, 2009, Sep-30, Volume: 42, Issue:9

    Topics: Acrylamide; Anti-Infective Agents; Cell Membrane; Dimerization; Escherichia coli; Fluorescence; Kinetics; Lipid Bilayers; Liposomes; Peptide Fragments; Peptides, Cyclic; Sodium Chloride; Staphylococcus aureus; Tryptophan

2009
Rhodotorula aurantiaca penicillin V acylase: active site characterization and fluorometric studies.
    Journal of photochemistry and photobiology. B, Biology, 2009, Nov-09, Volume: 97, Issue:2

    Topics: Acrylamide; Bromosuccinimide; Catalytic Domain; Circular Dichroism; Fluorescence; Kinetics; Penicillin Amidase; Phenylmethylsulfonyl Fluoride; Rhodotorula; Spectrometry, Fluorescence; Tryptophan

2009
Enantioseparation and amperometric detection of chiral compounds by in situ molecular imprinting on the microchannel wall.
    Analytical chemistry, 2009, Dec-01, Volume: 81, Issue:23

    Topics: Acrylamide; Chemical Fractionation; Cross-Linking Reagents; Electrochemistry; Methacrylates; Microfluidic Analytical Techniques; Molecular Imprinting; Stereoisomerism; Tryptophan

2009
Fluorescence quenching of buried Trp residues by acrylamide does not require penetration of the protein fold.
    The journal of physical chemistry. B, 2010, Jan-21, Volume: 114, Issue:2

    Topics: Acrylamide; Animals; Fish Proteins; Fishes; Fluorescence; Parvalbumins; Protein Conformation; Protein Folding; Proteins; Ribonuclease T1; Tryptophan

2010
Interaction with membrane mimics of transmembrane fragments 16 and 17 from the human multidrug resistance ABC transporter 1 (hMRP1/ABCC1) and two of their tryptophan variants.
    Biochimica et biophysica acta, 2010, Volume: 1798, Issue:3

    Topics: Acrylamide; Amino Acid Sequence; Anisotropy; Buffers; Cell Membrane; Circular Dichroism; Culture Media; Glucosides; Halogenation; Humans; Micelles; Molecular Mimicry; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutant Proteins; Peptide Fragments; Phosphorylcholine; Protein Binding; Protein Structure, Secondary; Spectrometry, Fluorescence; Time Factors; Titrimetry; Tryptophan

2010
The acrylamide (S)-2 as a positive and negative modulator of Kv7 channels expressed in Xenopus laevis oocytes.
    PloS one, 2009, Dec-11, Volume: 4, Issue:12

    Topics: Acrylamide; Acrylamides; Animals; Binding Sites; Carbamates; Humans; Ion Channel Gating; KCNQ Potassium Channels; Kinetics; Membrane Potentials; Mutant Proteins; Oocytes; Oxazines; Phenylenediamines; Tryptophan; Xenopus laevis

2009
Identification and characterization of molten globule-like state of hen egg-white lysozyme in presence of salts under alkaline conditions.
    Protein and peptide letters, 2010, Volume: 17, Issue:1

    Topics: Acrylamide; Animals; Chickens; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Muramidase; Potassium Chloride; Protein Conformation; Protein Denaturation; Protein Folding; Salts; Spectrometry, Fluorescence; Tryptophan

2010
The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.
    The Journal of biological chemistry, 2010, May-28, Volume: 285, Issue:22

    Topics: Acrylamide; Algorithms; Herpesvirus 1, Human; Histidine; Kinetics; Lipids; Liposomes; Magnetic Resonance Spectroscopy; Peptides; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Surface Plasmon Resonance; Tryptophan; Viral Envelope Proteins

2010
Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.
    European biophysics journal : EBJ, 2010, Volume: 39, Issue:10

    Topics: Acids; Acrylamide; Animals; Cattle; Ethylene Chlorohydrin; Fluorescence; Fluorescence Polarization; Hydrogen-Ion Concentration; Lactalbumin; Protein Denaturation; Protein Folding; Time Factors; Tryptophan

2010
Examining the influence of ultraviolet C irradiation on recombinant human γD-crystallin.
    Molecular vision, 2010, Dec-16, Volume: 16

    Topics: Acrylamide; Chemical Precipitation; Circular Dichroism; Disulfides; Electrophoresis, Polyacrylamide Gel; gamma-Crystallins; Guanidine; Humans; Molecular Weight; Nephelometry and Turbidimetry; Polymerization; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Solubility; Spectrometry, Fluorescence; Tryptophan; Ultraviolet Rays

2010
Amplitude spectrum of structural fluctuations in proteins from the internal diffusion of solutes of increasing molecular size: a Trp phosphorescence quenching study.
    Biochemistry, 2011, Feb-15, Volume: 50, Issue:6

    Topics: Acrylamide; Alcohol Dehydrogenase; Alkaline Phosphatase; Azurin; Diffusion; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Luminescent Measurements; Models, Molecular; Protein Conformation; Proteins; Solutions; Temperature; Tryptophan

2011
Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.
    Biochemistry, 2011, Mar-29, Volume: 50, Issue:12

    Topics: Acrylamide; Fluorescence Polarization; Phosphorylation; Phosphoserine; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan; Tyrosine 3-Monooxygenase

2011
Conformational changes of FtsZ reported by tryptophan mutants.
    Biochemistry, 2011, May-31, Volume: 50, Issue:21

    Topics: Acrylamide; Bacterial Proteins; Cytoskeletal Proteins; Microscopy, Electron; Models, Molecular; Mutation; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

2011
Mutational and structural studies of the PixD BLUF output signal that affects light-regulated interactions with PixE.
    Biochemistry, 2011, Jul-26, Volume: 50, Issue:29

    Topics: Acrylamide; Amino Acid Sequence; Bacterial Proteins; Chromatography, Gel; Crystallography, X-Ray; Darkness; Flavin-Adenine Dinucleotide; Fluorescence; Light; Light Signal Transduction; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Mutant Proteins; Mutation; Peptides; Photoreceptors, Microbial; Protein Binding; Protein Structure, Tertiary; Sequence Alignment; Solvents; Spectrophotometry, Ultraviolet; Synechocystis; Tryptophan

2011
Trifluoroethanol stabilizes the molten globule state and induces non-amyloidic turbidity in stem bromelain near its isoelectric point.
    International journal of biological macromolecules, 2011, Nov-01, Volume: 49, Issue:4

    Topics: Absorption; Acrylamide; Amyloid; Anilino Naphthalenesulfonates; Bromelains; Circular Dichroism; Enzyme Stability; Guanidine; Isoelectric Point; Nephelometry and Turbidimetry; Protein Binding; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Temperature; Trifluoroethanol; Tryptophan

2011
Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
    PloS one, 2012, Volume: 7, Issue:2

    Topics: Acrylamide; Amino Acid Motifs; Biophysics; Crystallography, X-Ray; Herpesvirus 1, Human; Lipids; Peptides; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan; Tyrosine; Viral Envelope Proteins

2012
Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl.
    International journal of biological macromolecules, 2012, Volume: 51, Issue:3

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Bromosuccinimide; Guanidine; Peanut Agglutinin; Protein Binding; Protein Denaturation; Protein Structure, Tertiary; Protein Unfolding; Temperature; Tryptophan; Urea

2012
Stabilization of ferrochelatase via lysine residues on the carboxyl terminal extension.
    Protein and peptide letters, 2013, Volume: 20, Issue:9

    Topics: Acrylamide; Animals; Chironomidae; Enzyme Stability; Ferrochelatase; Guanidine; Insect Proteins; Lysine; Mutation; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Structural Homology, Protein; Tryptophan

2013
Interaction with lipid II induces conformational changes in bovicin HC5 structure.
    Antimicrobial agents and chemotherapy, 2012, Volume: 56, Issue:9

    Topics: Acrylamide; Amino Acid Sequence; Bacteriocins; Circular Dichroism; Hydrogen-Ion Concentration; Membranes, Artificial; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Stability; Spectrometry, Fluorescence; Streptococcus bovis; Tryptophan; Uridine Diphosphate N-Acetylmuramic Acid

2012
Detection and analysis of protofibrils and fibrils of hemoglobin: implications for the pathogenesis and cure of heme loss related maladies.
    Archives of biochemistry and biophysics, 2013, Volume: 533, Issue:1-2

    Topics: Absorption; Acrylamide; Anilino Naphthalenesulfonates; Animals; Cattle; Dose-Response Relationship, Drug; Hematologic Diseases; Heme; Hemoglobins; Protein Multimerization; Spectrometry, Fluorescence; Trifluoroethanol; Tryptophan

2013
Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form.
    PloS one, 2013, Volume: 8, Issue:4

    Topics: Acids; Acrylamide; Anilino Naphthalenesulfonates; Chromatography, Gel; Circular Dichroism; Hydrodynamics; Hydrogen-Ion Concentration; Kinetics; Lectins; Light; Musa; Protein Binding; Protein Denaturation; Protein Multimerization; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Unfolding; Scattering, Radiation; Software; Spectrometry, Fluorescence; Temperature; Tryptophan; Urea

2013
Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
    FEBS letters, 2013, Aug-19, Volume: 587, Issue:16

    Topics: Acrylamide; alpha-Synuclein; Amino Acid Sequence; Cell Membrane; Humans; Lipid Bilayers; Lipids; Micelles; Molecular Sequence Data; Parkinson Disease; Phosphatidylcholines; Phosphatidylserines; Protein Binding; Protein Structure, Tertiary; Tryptophan

2013
Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies.
    Protein science : a publication of the Protein Society, 2013, Volume: 22, Issue:10

    Topics: Acrylamide; Antibodies, Monoclonal; Circular Dichroism; Fluorescence; Immunoglobulin G; Kinetics; Multiprotein Complexes; Protein Conformation; Protein Folding; Protein Multimerization; Protein Stability; Temperature; Tryptophan

2013
A comparative study of unfolding of Erythrina cristagalli Lectin in chemical denaturant and Fluoroalcohols.
    Protein and peptide letters, 2014, Volume: 21, Issue:1

    Topics: Acrylamide; Anilino Naphthalenesulfonates; Bromosuccinimide; Erythrina; Guanidine; Hydrogen-Ion Concentration; Oxidation-Reduction; Plant Lectins; Propanols; Protein Binding; Protein Denaturation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Trifluoroethanol; Tryptophan

2014
Thermally stable harpin, HrpZPss is sensitive to chemical denaturants: probing tryptophan environment, chemical and thermal unfolding by fluorescence spectroscopy.
    Biochimie, 2013, Volume: 95, Issue:12

    Topics: Acrylamide; Bacterial Outer Membrane Proteins; Calorimetry, Differential Scanning; Guanidine; Kinetics; Protein Denaturation; Protein Stability; Protein Unfolding; Spectrometry, Fluorescence; Tryptophan; Urea

2013
A molten globule intermediate of the von Willebrand factor A1 domain firmly tethers platelets under shear flow.
    Proteins, 2014, Volume: 82, Issue:5

    Topics: Acrylamide; Blood Platelets; Chromatography, Gel; Disulfides; Guanidine; Humans; Oxidation-Reduction; Platelet Adhesiveness; Protein Denaturation; Protein Structure, Tertiary; Rheology; Shear Strength; Spectrometry, Fluorescence; Temperature; Tryptophan; von Willebrand Factor

2014
Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.
    The journal of physical chemistry. B, 2014, Jun-12, Volume: 118, Issue:23

    Topics: Acrylamide; Alcohol Dehydrogenase; Bacterial Proteins; Biocatalysis; Catalytic Domain; Enzyme Stability; Fluorescence; Fluorescent Dyes; Geobacillus stearothermophilus; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tryptophan; Zinc

2014
Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms.
    Amino acids, 2014, Volume: 46, Issue:11

    Topics: 3T3 Cells; Acrylamide; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Drug Design; Erythrocytes; Humans; Leucine; Leucine Zippers; Lipids; Mice; Tryptophan

2014
Specific and ultrasensitive ciprofloxacin detection by responsive photonic crystal sensor.
    Journal of hazardous materials, 2014, Sep-15, Volume: 280

    Topics: Acrylamide; Ciprofloxacin; Hydrogen-Ion Concentration; Optics and Photonics; Osmolar Concentration; Tryptophan; Water Pollutants, Chemical; Zinc

2014
Insights into the membrane interaction mechanism and antibacterial properties of chensinin-1b.
    Biomaterials, 2015, Volume: 37

    Topics: Acrylamide; Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Cell Membrane; Cell Membrane Permeability; Circular Dichroism; Escherichia coli; Female; Fluoresceins; Hemolysis; Humans; Kinetics; Lipopolysaccharides; Liposomes; Mice; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides; Potassium Iodide; Protein Binding; Protein Structure, Secondary; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan; Wound Healing

2015
pH-induced structural change of a multi-tryptophan protein MPT63 with immunoglobulin-like fold: identification of perturbed tryptophan residue/residues.
    Journal of biomolecular structure & dynamics, 2015, Volume: 33, Issue:10

    Topics: Acrylamide; Amino Acid Motifs; Anilino Naphthalenesulfonates; Bacterial Proteins; Benzothiazoles; Cloning, Molecular; Escherichia coli; Fluorescent Dyes; Gene Expression; Hydrogen Bonding; Hydrogen-Ion Concentration; Immunoglobulins; Molecular Sequence Data; Mycobacterium tuberculosis; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Spectrometry, Fluorescence; Static Electricity; Thermodynamics; Thiazoles; Tryptophan; Tyrosine

2015
Spectroscopic Characterization of Structural Changes in Membrane Scaffold Proteins Entrapped within Mesoporous Silica Gel Monoliths.
    ACS applied materials & interfaces, 2015, Apr-29, Volume: 7, Issue:16

    Topics: Acrylamide; Amino Acid Sequence; Anisotropy; Circular Dichroism; Lipoproteins; Membrane Proteins; Molecular Sequence Data; Nanoparticles; Porosity; Silica Gel; Solutions; Spectrometry, Fluorescence; Tryptophan

2015
Insights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.
    PloS one, 2015, Volume: 10, Issue:11

    Topics: Acrylamide; Amyloid; Animals; Benzothiazoles; Chickens; Chromatography, High Pressure Liquid; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Light; Microscopy, Atomic Force; Muramidase; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Scattering, Radiation; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Thiazoles; Time Factors; Tryptophan

2015
Carbonyl-based blue autofluorescence of proteins and amino acids.
    PloS one, 2017, Volume: 12, Issue:5

    Topics: Acrylamide; Amino Acids; Fluorescence; Lactoglobulins; Optical Imaging; Proline; Proteins; Solutions; Spectrometry, Fluorescence; Tryptophan

2017
Triplet state spectroscopy reveals involvement of the buried tryptophan residue 310 in Glyceraldehyde-3-phosphate dehydrogenase (GAPD) in the interaction with acrylamide.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2024, Feb-15, Volume: 307

    Topics: Acrylamide; Animals; Glyceraldehyde-3-Phosphate Dehydrogenases; Molecular Docking Simulation; Rabbits; Spectrometry, Fluorescence; Tryptophan

2024