guanidine and cytochrome c-t

guanidine has been researched along with cytochrome c-t in 81 studies

Research

Studies (81)

Timeframe	Studies, this research(%)	All Research%
pre-1990	9 (11.11)	18.7374
1990's	9 (11.11)	18.2507
2000's	41 (50.62)	29.6817
2010's	18 (22.22)	24.3611
2020's	4 (4.94)	2.80

Authors

Authors	Studies
Hickey, DR; McLendon, G; Sherman, F	1
Nall, BT; Osterhout, JJ; Ramdas, L	1
Nall, BT; Ramdas, L; White, TB; Wood, LC	1
Muthukrishnan, K; Nall, BT; Osterhout, JJ	1
Nall, BT; Ramdas, L; Sherman, F	1
Nall, BT; Ramdas, L	1
Landers, TA; Nall, BT	1
Nall, BT; Zuniga, EH	1
Linske-O'Connell, LI; McLendon, G; Sherman, F	1
Bowler, BE; Caughey, WS; Dong, A	1
Nall, BT; Veeraraghavan, S	1
Auld, DS; Betz, SF; Doyle, DF; Pielak, GJ; Saunders, AJ; Young, GB	1
Alcazar-Roman, L; Doyle, DF; Parikh, S; Pielak, GJ; Waldner, JC	1
Bowler, BE; Dong, A; Garbin, K; Godbole, S	1
Fetrow, JS; Qu, K; Scholes, CP; Sienkiewicz, A; Vaughn, JL	1
Bowler, BE; Godbole, S	1
Attfield, K; Bowler, BE; Clayton, D; Dec, E; Dong, A; Hammack, B; Sarisky, C	1
Bowler, BE; Godbole, S; Hammack, B	1
Nall, BT; Pierce, MM	1
Bowler, BE; Hammack, BN; Smith, CR	1
Bowler, BE; Smith, CR; Wandschneider, E	1
Chang, IJ; Gray, HB; Lee, JC; Winkler, JR	1
Brunori, M; Gianni, S; Morea, V; Soulimane, T; Tramontano, A; Travaglini-Allocatelli, C	1
Nada, T; Terazima, M	1
Bowler, BE; Hammack, BN; Wandschneider, E	1
HORIO, T; OKUNUKI, K; YAMANAKA, T	1
Antalík, M; Bánó, M; Varhac, R	1
Bhuyan, AK; Kumar, R; Prabhu, NP	1
Bowler, BE; Ford, CD; Zhang, MM	1
Bowler, BE; Wandschneider, E	1
Bartalesi, I; Bertini, I; Di Rocco, G; Ranieri, A; Rosato, A; Vanarotti, M; Vasos, PR; Viezzoli, MS	1
Chen, E; Goldbeck, RA; Kliger, DS	1
Bhuyan, AK; Kumar, R; Prabhu, NP; Yadaiah, M	1
Nada, T; Nishida, S; Terazima, M	2
Bowler, BE; Kristinsson, R	1
Bhuyan, AK; Kumar, R	1
Bhuyan, AK; Prabhu, NP; Rao, DK	1
Baddam, S; Bowler, BE	1
Ishimori, K; Kimura, T; Morishima, I; Sakamoto, K	1
Cheng, H; Latypov, RF; Roder, H; Roder, NA; Zhang, J	1
Bhuyan, AK; Kumar, R; Rao, DK; Yadaiah, M	1
Jiang, M; Liang, L; Yao, P	1
Bhuyan, AK; Kumar, R; Prabhu, NP; Rao, DK	1
Dai, SY; Fitzgerald, MC	1
He, F; Liu, X; Luo, D; Wang, C; Wang, H; Xia, C; Yuan, L	1
Bhuyan, AK; Kumar, R; Yadaiah, M	1
Agueci, F; Fiorucci, L; Piro, MC; Polticelli, F; Santucci, R; Sinibaldi, F	1
Bowler, BE; Kurchan, E; Tzul, FO	1
Baddam, S; Bandi, S; Bowler, BE	1
Kawano, S; Tai, H; Yamamoto, Y	1
Abel, CJ; Chen, E; Goldbeck, RA; Kliger, DS	1
Ahmad, F; Hassan, I; Khan, KA; Moosavi-Movahedi, AA; Rahaman, H; Singh, SB; Singh, TP; Wahid, M	1
Hasegawa, J; Kobayashi, Y; Nakamura, S; Sambongi, Y; Sonoyama, T; Uchiyama, S	1
Munegumi, T; Tai, H; Yamamoto, Y	1
Bowler, BE; Kurchan, E; Roder, H; Tzul, FO	1
Bryan, MA; Sharp, KA; Vanderkooi, JM; Zelent, B	1
Dawson, PE; Romesberg, FE; Thielges, MC; Zimmermann, J	1
Romesberg, FE; Thielges, MC; Zimmermann, J	1
Sinz, A; Spross, J	1
Cheung, MS; Christiansen, A; Samiotakis, A; Wang, Q; Wittung-Stafshede, P	1
Bischin, C; Cooper, CE; Damian, G; Deac, F; Rajagopal, BS; Silaghi-Dumitrescu, R; Worrall, JA	1
Bowler, BE; Finnegan, ML	1
Jain, R; Kaur, S; Kumar, R	1
Bowler, BE; Khan, MK	1
Kim, J; Lee, T; Lim, M; Pak, Y; Park, J	1
Champion, PM; Karunakaran, V; Sun, Y	1
Bhuyan, AK; Sashi, P; Yasin, UM	1
Beck, WF; Mueller, JJ; Shepherd, NC; Tripathy, J	1
Bian, L; Ji, X	1
Basak, P; Bhattacharyya, M; Kundu, N; Pattanayak, R	1
Agarwal, MC; Chhabra, R; Jain, R; Kumar, R; Kumar, S	1
Ahmad, F; Batra, JK; Haque, MA; Hassan, MI; Islam, A; Prakash, A; Ubaid-Ullah, S; Zaidi, S	1
Bowler, BE; Briknarova, K; Danielson, TA; Dar, TA; Stine, JM	1
Bowler, BE; Danielson, TA	1
Bowler, BE; Cherney, MM; Finnegan, ML; Leavens, MJ	1
Kumar, R; Kumar, V; Sharma, D	1
Ahmad, F; Hassan, MI; Islam, A; Khan, SH; Lynn, AM; Pandey, P; Prakash, A	1
Bowler, BE; Cherney, MM; Leavens, MJ; Spang, LE	1
Bhattacharya, S; Cazade, PA; Gamero-Quijano, A; Herzog, G; Scanlon, MD; Thompson, D; Walsh, S	1
Garg, M; Kumar, R; Sharma, D	1

Other Studies

81 other study(ies) available for guanidine and cytochrome c-t

Article	Year
Thermodynamic stabilities of yeast iso-1-cytochromes c having amino acid substitutions for lysine 32. The Journal of biological chemistry, 1988, Dec-05, Volume: 263, Issue:34 Topics: Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Guanidines; Kinetics; Lysine; Protein Denaturation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry; Thermodynamics	1988
pH dependence of folding of iso-2-cytochrome c. Biochemistry, 1988, Sep-20, Volume: 27, Issue:19 Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry	1988
Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-2-cytochrome c. Biochemistry, 1988, Nov-15, Volume: 27, Issue:23 Topics: Cytochrome c Group; Cytochromes c; Glycine; Guanidine; Guanidines; Kinetics; Models, Molecular; Proline; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Fluorescence	1988
pH-induced conformation changes and equilibrium unfolding in yeast iso-2 cytochrome c. Biochemistry, 1985, Nov-05, Volume: 24, Issue:23 Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Protein Conformation; Protein Denaturation; Saccharomyces cerevisiae	1985
Guanidine hydrochloride induced equilibrium unfolding of mutant forms of iso-1-cytochrome c with replacement of proline-71. Biochemistry, 1986, Nov-04, Volume: 25, Issue:22 Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	1986
Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71. Biochemistry, 1986, Nov-04, Volume: 25, Issue:22 Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins	1986
Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c. Biochemistry, 1981, Sep-15, Volume: 20, Issue:19 Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry; Temperature; Thermodynamics	1981
Folding of yeast iso-1-AM cytochrome c. Biochemistry, 1983, Mar-15, Volume: 22, Issue:6 Topics: Amino Acids; Autoradiography; Chemical Phenomena; Chemistry; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Peptide Fragments; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry; Sulfhydryl Compounds	1983
Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochrome c: in vivo and in vitro effects. Biochemistry, 1995, May-30, Volume: 34, Issue:21 Topics: Amino Acid Sequence; Amino Acids; Base Sequence; Calorimetry, Differential Scanning; Cytochrome c Group; Cytochromes c; DNA, Fungal; Guanidine; Guanidines; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	1995
Characterization of the guanidine hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy. Biochemistry, 1994, Mar-08, Volume: 33, Issue:9 Topics: Amides; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Protein Denaturation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry, Infrared; Structure-Activity Relationship; Thermodynamics	1994
Characterization of folding intermediates using prolyl isomerase. Biochemistry, 1994, Jan-25, Volume: 33, Issue:3 Topics: Amino Acid Isomerases; Carrier Proteins; Catalysis; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Models, Chemical; Mutation; Peptidylprolyl Isomerase; Proline; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Time Factors	1994
Probing weakly polar interactions in cytochrome c. Protein science : a publication of the Protein Society, 1993, Volume: 2, Issue:12 Topics: Cysteine; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Tyrosine	1993
Changing the transition state for protein (Un) folding. Biochemistry, 1996, Jun-11, Volume: 35, Issue:23 Topics: Asparagine; Calorimetry; Circular Dichroism; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Guanidines; Isoleucine; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sensitivity and Specificity; Thermodynamics	1996
A lysine 73-->histidine variant of yeast iso-1-cytochrome c: evidence for a native-like intermediate in the unfolding pathway and implications for m value effects. Biochemistry, 1997, Jan-07, Volume: 36, Issue:1 Topics: Circular Dichroism; Cytochrome c Group; Cytochromes c; Fluorescence; Fungal Proteins; Guanidine; Guanidines; Hydrogen-Ion Concentration; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Thermodynamics; Tryptophan; Urea	1997
Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102. Biochemistry, 1997, Mar-11, Volume: 36, Issue:10 Topics: Circular Dichroism; Cysteine; Cytochrome c Group; Cytochromes c; Electron Spin Resonance Spectroscopy; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Mesylates; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry; Spin Labels; Temperature; Thermodynamics	1997
Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys 73 --> His variant of yeast iso-1-cytochrome c. Biochemistry, 1999, Jan-05, Volume: 38, Issue:1 Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Guanidine; Histidine; Hydrogen-Ion Concentration; Lysine; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry	1999
The magnitude of changes in guanidine-HCl unfolding m-values in the protein, iso-1-cytochrome c, depends upon the substructure containing the mutation. Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:8 Topics: Circular Dichroism; Cytochrome c Group; Cytochromes c; Guanidine; Hydrochloric Acid; Methionine; Models, Molecular; Molecular Structure; Mutagenesis; Protein Folding; Saccharomyces cerevisiae Proteins; Solvents; Spectrum Analysis; Static Electricity; Thermodynamics	1998
Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c. Journal of molecular biology, 2000, Feb-11, Volume: 296, Issue:1 Topics: Binding, Competitive; Biopolymers; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry	2000
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization. Journal of molecular biology, 2000, May-19, Volume: 298, Issue:5 Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochrome c Group; Cytochromes c; Enzyme Stability; Fluorescence; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Proline; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae; Sequence Alignment; Thermodynamics	2000
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors. Journal of molecular biology, 2001, Aug-31, Volume: 311, Issue:5 Topics: Acetylation; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Mutation; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Serine Endopeptidases; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thermodynamics; Titrimetry; Yeasts	2001
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation. Biochemistry, 2003, Feb-25, Volume: 42, Issue:7 Topics: Acetylation; Amino Acid Substitution; Binding, Competitive; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Spectrometry, Fluorescence; Tryptophan	2003
The protein-folding speed limit: intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c. Proceedings of the National Academy of Sciences of the United States of America, 2003, Apr-01, Volume: 100, Issue:7 Topics: Cytochrome c Group; Cytochromes c; Electron Transport; Guanidine; Histidine; Kinetics; Macromolecular Substances; Metalloporphyrins; Models, Molecular; Organometallic Compounds; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Ruthenium; Sucrose; Time Factors; Zinc	2003
Exploring the cytochrome c folding mechanism: cytochrome c552 from thermus thermophilus folds through an on-pathway intermediate. The Journal of biological chemistry, 2003, Oct-17, Volume: 278, Issue:42 Topics: Cytochrome c Group; Cytochromes c; Dose-Response Relationship, Drug; Guanidine; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Temperature; Thermodynamics; Thermus thermophilus	2003
A novel method for study of protein folding kinetics by monitoring diffusion coefficient in time domain. Biophysical journal, 2003, Volume: 85, Issue:3 Topics: Biophysics; Cytochromes c; Diffusion; Electrons; Guanidine; Kinetics; Light; Models, Chemical; Protein Folding; Temperature; Time Factors	2003
Evaluation of cooperative interactions between substructures of iso-1-cytochrome c using double mutant cycles. Biochemistry, 2003, Sep-16, Volume: 42, Issue:36 Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Histidine; Isoenzymes; Isoleucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	2003
Effects of guanidine salts on the spectral properties of cytochrome c. Journal of biochemistry, 1962, Volume: 51 Topics: Amidines; Cytochromes; Cytochromes c; Guanidine; Guanidines; Salts	1962
Effect of temperature and guanidine hydrochloride on ferrocytochrome c at neutral pH. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2004, Volume: 9, Issue:1 Topics: Animals; Calorimetry, Differential Scanning; Cytochromes c; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Protein Denaturation; Protein Structure, Tertiary; Spectrophotometry, Atomic; Temperature; Transition Temperature; Viscosity	2004
Folding barrier in horse cytochrome c: support for a classical folding pathway. Journal of molecular biology, 2004, Mar-12, Volume: 337, Issue:1 Topics: Animals; Carbon Monoxide; Cytochromes c; Electron Spin Resonance Spectroscopy; Guanidine; Horses; Nitroso Compounds; Protein Conformation; Protein Folding; Thermodynamics	2004
Estimation of the compaction of the denatured state by a protein variant involved in a reverse hydrophobic effect. The protein journal, 2004, Volume: 23, Issue:2 Topics: Amino Acid Substitution; Cytochromes c; Genetic Variation; Guanidine; Hydrophobic and Hydrophilic Interactions; Isoenzymes; Mutation; Protein Denaturation; Saccharomyces cerevisiae Proteins	2004
Conformational properties of the iso-1-cytochrome C denatured state: dependence on guanidine hydrochloride concentration. Journal of molecular biology, 2004, May-21, Volume: 339, Issue:1 Topics: Cytochromes c; Guanidine; Heme; Histidine; Isoenzymes; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins	2004
Protein stability and mutations in the axial methionine loop of a minimal cytochrome c. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2004, Volume: 9, Issue:5 Topics: Amino Acids; Bacillus; Cytochromes c; Enzyme Stability; Guanidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Protein Denaturation; Protein Folding; Thermodynamics; Water	2004
The earliest events in protein folding: a structural requirement for ultrafast folding in cytochrome C. Journal of the American Chemical Society, 2004, Sep-15, Volume: 126, Issue:36 Topics: Animals; Cytochromes c; Ferric Compounds; Guanidine; Histidine; Kinetics; Metalloproteins; Myocardium; NAD; Optical Rotation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Tuna	2004
Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride. Biophysical journal, 2004, Volume: 87, Issue:4 Topics: Carbon Monoxide; Cytochromes c; Elasticity; Entropy; Enzyme Activation; Enzyme Stability; Guanidine; Hydrogen-Ion Concentration; Protein Conformation; Protein Denaturation; Protein Folding; Solutions	2004
Kinetics of intermolecular interaction during protein folding of reduced cytochrome c. Biophysical journal, 2004, Volume: 87, Issue:4 Topics: Carbon Monoxide; Computer Simulation; Cytochromes c; Diffusion; Elasticity; Entropy; Enzyme Activation; Enzyme Stability; Guanidine; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Models, Chemical; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Solutions; Solvents	2004
Communication of stabilizing energy between substructures of a protein. Biochemistry, 2005, Feb-22, Volume: 44, Issue:7 Topics: Amino Acid Substitution; Asparagine; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Hydrogen-Ion Concentration; Isoenzymes; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Temperature; Thermodynamics	2005
Two-state folding of horse ferrocytochrome c: analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics. Biochemistry, 2005, Mar-01, Volume: 44, Issue:8 Topics: Animals; Cytochromes c; Guanidine; Horses; Indicators and Reagents; Kinetics; Protein Denaturation; Protein Folding; Thermodynamics; Urea	2005
Protein folding in classical perspective: folding of horse cytochrome c. Biochemistry, 2005, Mar-01, Volume: 44, Issue:8 Topics: Animals; Calorimetry; Cytochromes c; Dithionite; Guanidine; Horses; Kinetics; Magnetic Resonance Spectroscopy; Models, Biological; Protein Denaturation; Protein Folding	2005
Hydrogen bonding dynamics during protein folding of reduced cytochrome c: temperature and denaturant concentration dependence. Biophysical journal, 2005, Volume: 89, Issue:3 Topics: Animals; Biophysics; Cytochromes c; Diffusion; Dose-Response Relationship, Drug; Guanidine; Horses; Hydrogen Bonding; Kinetics; Ligands; Macromolecular Substances; Models, Statistical; Myocardium; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Protein Structure, Tertiary; Temperature; Thermodynamics; Time Factors	2005
Thermodynamics and kinetics of formation of the alkaline state of a Lys 79-->Ala/Lys 73-->His variant of iso-1-cytochrome c. Biochemistry, 2005, Nov-15, Volume: 44, Issue:45 Topics: Alanine; Cytochromes c; Guanidine; Histidine; Hydrogen-Ion Concentration; Kinetics; Lysine; Mutagenesis, Site-Directed; Proline; Protein Denaturation; Saccharomyces cerevisiae Proteins; Static Electricity; Thermodynamics	2005
Dehydration in the folding of reduced cytochrome c revealed by the electron-transfer-triggered folding under high pressure. Journal of the American Chemical Society, 2006, Jan-25, Volume: 128, Issue:3 Topics: Cytochromes c; Guanidine; Heme; Hydrophobic and Hydrophilic Interactions; Kinetics; Oxidation-Reduction; Pressure; Protein Folding; Water	2006
Structural characterization of an equilibrium unfolding intermediate in cytochrome c. Journal of molecular biology, 2006, Mar-31, Volume: 357, Issue:3 Topics: Amino Acid Substitution; Animals; Cytochromes c; Guanidine; Horses; Protein Denaturation; Protein Folding; Spectrophotometry; Urea	2006
The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. Biochemistry, 2006, Mar-14, Volume: 45, Issue:10 Topics: Alkalies; Carbon Monoxide; Circular Dichroism; Cytochromes c; Enzyme Stability; Guanidine; Kinetics; Molecular Conformation; Photolysis; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sodium Chloride; Spectrophotometry, Ultraviolet	2006
Reversibility of structural transition of cytochrome c on interacting with and releasing from alternating copolymers of maleic Acid and alkene. Biomacromolecules, 2006, Volume: 7, Issue:6 Topics: Alkenes; Animals; Cytochromes c; Guanidine; Heart; Horses; Hydrogen-Ion Concentration; Maleates; Microscopy, Atomic Force; Osmolar Concentration; Polymers; Protein Conformation; Protein Structure, Secondary; Sensitivity and Specificity; Sodium Chloride; Static Electricity; Structure-Activity Relationship; Temperature	2006
The alkali molten globule state of horse ferricytochrome c: observation of cold denaturation. Journal of molecular biology, 2006, Dec-01, Volume: 364, Issue:3 Topics: Animals; Cold Temperature; Cytochromes c; Guanidine; Heating; Horses; Hydrogen-Ion Concentration; Protein Conformation; Protein Denaturation; Sodium Hydroxide	2006
A mass spectrometry-based probe of equilibrium intermediates in protein-folding reactions. Biochemistry, 2006, Oct-24, Volume: 45, Issue:42 Topics: Animals; Cattle; Cytochromes c; Deuterium Oxide; Fatty Acid-Binding Proteins; Guanidine; Kinetics; Lactalbumin; Mass Spectrometry; Protein Folding; Thermodynamics; Urea	2006
Quantitative analysis of cytochrome C released from rice mitochondria using the adsorptive polarographic wave of guanidine modified Co(II)-cytochrome C complex. Protein and peptide letters, 2006, Volume: 13, Issue:8 Topics: Amino Acids; Cobalt; Cytochromes c; Guanidine; Mitochondria; Monosaccharides; Oryza; Polarography; Reproducibility of Results; Sodium Hydroxide; Sulfites	2006
Glassy dynamics in the folding landscape of cytochrome c detected by laser photolysis. Biochemistry, 2007, Mar-06, Volume: 46, Issue:9 Topics: Cytochromes c; Guanidine; Kinetics; Lasers; Photolysis; Protein Folding	2007
Probing the effect of mutations on cytochrome C stability. Protein and peptide letters, 2007, Volume: 14, Issue:4 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cytochromes c; Enzyme Stability; Guanidine; Horses; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins	2007
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts. Journal of molecular biology, 2007, Aug-17, Volume: 371, Issue:3 Topics: Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Insertional; Mutant Proteins; Peptides; Protein Denaturation; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry	2007
Alkaline conformational transition and gated electron transfer with a Lys 79 --> his variant of iso-1-cytochrome c. Biochemistry, 2007, Sep-18, Volume: 46, Issue:37 Topics: Alkalies; Anaerobiosis; Cytochromes c; Electron Transport; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Magnetic Resonance Spectroscopy; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	2007
Characterization of N-terminal amino group-heme ligation emerging upon guanidine hydrochloric acid induced unfolding of Hydrogenobacter thermophilus ferricytochrome c552. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008, Volume: 13, Issue:1 Topics: Acids; Bacteria; Circular Dichroism; Cytochromes c; Guanidine; Heme; Hydrogen-Ion Concentration; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Spectrophotometry, Ultraviolet	2008
Non-native heme-histidine ligation promotes microsecond time scale secondary structure formation in reduced horse heart cytochrome c. Biochemistry, 2007, Oct-30, Volume: 46, Issue:43 Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Heme; Histidine; Horses; Myocardium; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet	2007
Sequence and stability of the goat cytochrome c. Biophysical chemistry, 2008, Volume: 138, Issue:1-2 Topics: Amino Acid Sequence; Animals; Base Sequence; Cattle; Circular Dichroism; Cytochromes c; Goats; Guanidine; Hot Temperature; Models, Biological; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Temperature; Thermodynamics	2008
Stability enhancement of cytochrome c through heme deprotonation and mutations. Biophysical chemistry, 2009, Volume: 139, Issue:1 Topics: Bacterial Proteins; Cytochromes c; Guanidine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Mutation; Protein Denaturation; Protein Stability; Protons; Pseudomonas aeruginosa	2009
Stability of the heme Fe-N-terminal amino group coordination bond in denatured cytochrome c. Inorganic chemistry, 2009, Jan-05, Volume: 48, Issue:1 Topics: Amino Acid Sequence; Aquifoliaceae; Cytochromes c; Electrons; Guanidine; Heme; Histidine; Iron; Magnetic Resonance Spectroscopy; Mutation; Nitrogen; Oxidation-Reduction; Protein Denaturation; Pseudomonas aeruginosa	2009
Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c. Biochemistry, 2009, Jan-20, Volume: 48, Issue:2 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Ligands; Models, Chemical; Molecular Sequence Data; Mutation; Protein Binding; Protein Denaturation; Protein Multimerization; Protein Renaturation; Protein Structure, Secondary; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Temperature	2009
Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy. Biophysical chemistry, 2009, Volume: 141, Issue:2-3 Topics: Ammonium Chloride; Animals; Antifreeze Proteins; Cattle; Cytochromes c; Flounder; Freezing; Glutamic Acid; Guanidine; Methanol; Methylamines; Peptides; Polylysine; Proteins; Serum Albumin, Bovine; Sodium Acetate; Spectrophotometry, Infrared; Temperature; Transition Temperature; Urea; Water	2009
The determinants of stability and folding in evolutionarily diverged cytochromes c. Journal of molecular biology, 2009, Apr-24, Volume: 388, Issue:1 Topics: Cytochromes c; Evolution, Molecular; Guanidine; Kinetics; Models, Molecular; Protein Conformation; Protein Folding	2009
Direct observation of ligand dynamics in cytochrome c. Journal of the American Chemical Society, 2009, May-06, Volume: 131, Issue:17 Topics: Animals; Carbon Monoxide; Cytochromes c; Guanidine; Horses; Ligands; Protein Denaturation; Protein Folding; Spectroscopy, Fourier Transform Infrared; Thermodynamics; Time Factors	2009
A capillary monolithic trypsin reactor for efficient protein digestion in online and offline coupling to ESI and MALDI mass spectrometry. Analytical chemistry, 2010, Feb-15, Volume: 82, Issue:4 Topics: Acetonitriles; Analytic Sample Preparation Methods; Animals; Cattle; Cytochromes c; Enzymes, Immobilized; Guanidine; Humans; Muramidase; Online Systems; Polymers; Protein Denaturation; Proteins; Serum Albumin, Bovine; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin; Urea	2010
Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c. Biochemistry, 2010, Aug-10, Volume: 49, Issue:31 Topics: Circular Dichroism; Computer Simulation; Cytochromes c; Dextrans; Ficoll; Guanidine; Hot Temperature; Macromolecular Substances; Protein Stability; Protein Structure, Secondary	2010
Ascorbate peroxidase activity of cytochrome c. Free radical research, 2011, Volume: 45, Issue:4 Topics: Animals; Apoptosis; Ascorbic Acid; Cardiolipins; Cattle; Cytochrome-c Peroxidase; Cytochromes c; Free Radicals; Guanidine; Heme; Horses; Hydrogen Peroxide; Iron; Kinetics; Methylation; Mitochondria, Heart; Signal Transduction; Spectrum Analysis; Yeasts	2011
Scaling properties of glycine-rich sequences in guanidine hydrochloride solutions. Biophysical journal, 2012, Apr-18, Volume: 102, Issue:8 Topics: Cytochromes c; Glycine; Guanidine; Kinetics; Peptide Fragments; Protein Denaturation; Protein Stability; Solutions; Thermodynamics	2012
Guanidine hydrochloride-induced alkali molten globule model of horse ferrocytochrome c. Journal of biochemistry, 2013, Volume: 153, Issue:2 Topics: Animals; Carbon Monoxide; Circular Dichroism; Cytochromes c; Guanidine; Horses; Sodium Chloride	2013
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions. Biophysical journal, 2012, Nov-07, Volume: 103, Issue:9 Topics: Alanine; Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Insertional; Peptides; Protein Denaturation; Protein Stability; Protein Structure, Tertiary	2012
Dynamics of geminate rebinding of CO to cytochrome c in guanidine HCl probed by femtosecond vibrational spectroscopy. The journal of physical chemistry. B, 2013, May-02, Volume: 117, Issue:17 Topics: Carbon Isotopes; Carbon Monoxide; Cytochromes c; Deuterium Oxide; Guanidine; Protein Binding; Protein Denaturation; Spectroscopy, Fourier Transform Infrared; Time Factors	2013
Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding. The journal of physical chemistry. B, 2013, Aug-22, Volume: 117, Issue:33 Topics: Animals; Cytochromes c; Guanidine; Heme; Horses; Hydrogen-Ion Concentration; Models, Molecular; Protein Denaturation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Temperature; Thermodynamics	2013
Expansion and internal friction in unfolded protein chain. The journal of physical chemistry. B, 2013, Oct-10, Volume: 117, Issue:40 Topics: Carbon Monoxide; Cytochromes c; Guanidine; Hydrodynamics; Magnetic Resonance Spectroscopy; Photolysis; Protein Denaturation	2013
Dynamic solvation and coupling of the hydration shell of Zn(II)-substituted cytochrome c in the presence of guanidinium ions. The journal of physical chemistry. B, 2013, Nov-27, Volume: 117, Issue:47 Topics: Animals; Cytochromes c; Guanidine; Horses; Hydrogen Bonding; Ions; Models, Molecular; Protein Conformation; Spectrometry, Fluorescence; Zinc	2013
Distribution, transition and thermodynamic stability of protein conformations in the denaturant-induced unfolding of proteins. PloS one, 2014, Volume: 9, Issue:3 Topics: Animals; Carbonic Anhydrases; Cattle; Chickens; Cytochromes c; Guanidine; Muramidase; Myocardium; Protein Conformation; Protein Denaturation; Protein Unfolding; Regression Analysis; Thermodynamics; Urea	2014
Denaturation properties and folding transition states of leghemoglobin and other heme proteins. Biochemistry. Biokhimiia, 2015, Volume: 80, Issue:4 Topics: Arachis; Cytochromes c; Guanidine; Leghemoglobin; Myoglobin; Protein Denaturation; Protein Folding; Spectrum Analysis; Urea	2015
Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c. Archives of biochemistry and biophysics, 2015, Nov-01, Volume: 585 Topics: Amino Acid Sequence; Animals; Cytochromes c; Guanidine; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Myocardium; Protein Denaturation; Protein Folding; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Unfolding; Static Electricity; Thermodynamics; Urea	2015
Denatured states of yeast cytochrome c induced by heat and guanidinium chloride are structurally and thermodynamically different. Journal of biomolecular structure & dynamics, 2017, Volume: 35, Issue:7 Topics: Amino Acid Sequence; Animals; Cloning, Molecular; Cytochromes c; Gene Expression; Genetic Vectors; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Molecular Dynamics Simulation; Protein Denaturation; Protein Folding; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Deletion; Thermodynamics	2017
Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c. Biochemistry, 2017, 12-26, Volume: 56, Issue:51 Topics: Cytochromes c; Guanidine; Histidine; Lysine; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Thermodynamics	2017
Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'. Biophysical journal, 2018, 01-23, Volume: 114, Issue:2 Topics: Cytochromes c; Guanidine; Heme; Kinetics; Models, Molecular; Mutagenesis; Protein Conformation, alpha-Helical; Protein Denaturation; Rhodopseudomonas	2018
Probing Denatured State Conformational Bias in a Three-Helix Bundle, UBA(2), Using a Cytochrome c Fusion Protein. Biochemistry, 2018, 03-20, Volume: 57, Issue:11 Topics: Cytochromes c; Guanidine; Kinetics; Models, Molecular; Molecular Probes; Protein Conformation; Protein Denaturation; Recombinant Fusion Proteins; Rhodopseudomonas; Thermodynamics; Ubiquitin-Activating Enzymes	2018
Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro. Archives of biochemistry and biophysics, 2018, 09-15, Volume: 654 Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Hemeproteins; Horses; Kinetics; Macromolecular Substances; Myoglobin; Protein Denaturation; Protein Stability; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Thermodynamics; Viscosity	2018
Effects of natural mutations (L94I and L94V) on the stability and mechanism of folding of horse cytochrome c: A combined in vitro and molecular dynamics simulations approach. International journal of biological macromolecules, 2020, Sep-15, Volume: 159 Topics: Amino Acid Substitution; Animals; Cytochromes c; Guanidine; Horses; Molecular Dynamics Simulation; Mutation; Protein Denaturation; Protein Folding; Spectrum Analysis; Thermodynamics; Urea	2020
Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues. Biochemistry, 2021, 10-19, Volume: 60, Issue:41 Topics: Cytochromes c; Guanidine; Kinetics; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Denaturation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	2021
On the origin of chaotrope-modulated electrocatalytic activity of cytochrome Chemical communications (Cambridge, England), 2022, Mar-08, Volume: 58, Issue:20 Topics: Cytochromes c; Guanidine; Reactive Oxygen Species; Urea; Water	2022
Analysis of the effect of 1-Allyl-3-Methylimidazolium chloride on thermodynamic stability, folding kinetics, and motional dynamics of horse cytochrome c. Biophysical chemistry, 2022, Volume: 290 Topics: Allyl Compounds; Animals; Chlorides; Cytochromes c; Guanidine; Horses; Imidazoles; Kinetics; Protein Denaturation; Protein Folding; Solvents; Sphingosine; Thermodynamics	2022