cysteine has been researched along with 1,5-i-aedans in 53 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 12 (22.64) | 18.7374 |
| 1990's | 31 (58.49) | 18.2507 |
| 2000's | 8 (15.09) | 29.6817 |
| 2010's | 2 (3.77) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Stoffel, W; Weimbs, T | 1 |
| Brand, L; James, E; Stites, W; Wu, PG | 1 |
| Alvear, M; Cardemil, E; Encinas, MV; Kemp, RG; Latshaw, SP | 1 |
| Fromm, HJ; Soans, C | 1 |
| Itoh, M; Kimura, K; Nakano, Y; Tanaka, E | 1 |
| Baty, D; Lakey, JH; Pattus, F | 1 |
| Cyran, FP; Fisher, MT; Ginsburg, A; Han, MK; Kim, SH | 1 |
| Seifried, SE; von Hippel, PH; Wang, Y | 1 |
| Chou, WY; Matthews, KS | 1 |
| Pont-Lezica, RF; Varner, JE | 1 |
| González, G | 1 |
| Barden, JA; dos Remedios, CG; Hambly, BD; Miki, M | 1 |
| Andley, UP | 1 |
| Gorman, JJ | 1 |
| Barden, JA; dos Remedios, CG; Miki, M | 1 |
| Miki, M; Wahl, P | 1 |
| Moss, DJ; Trentham, DR | 1 |
| Barrett, CI; Schneider, JM; York, SS | 1 |
| Gennis, RB; Koland, JG | 1 |
| Abate-Shen, C; Curran, T; Isaac, VE; Patel, L | 1 |
| Dirr, H; Sluis-Cremer, N | 1 |
| Crews, BC; Gettins, PG | 1 |
| Honma, M; Kawai, J; Yamada, M | 1 |
| Duong, AM; Reisler, E | 1 |
| dos Remedios, CG; Moens, PD; Yee, DJ | 1 |
| Alvear, M; Cardemil, E; Encinas, MV; Herrera, L | 1 |
| Cash, VL; Dean, DR; White, RH; Zheng, L | 1 |
| Bautsch, W; Emde, M; Federwisch, M; Klos, A; Köhl, J; Melcher, T; Stühmer, T; Wollmer, A | 1 |
| Fink, AL; Goto, Y; Hamada, D; Hoshino, M; Kataoka, M | 1 |
| Khaitlina, S; Moraczewska, J; Mossakowska, M; Strzelecka-Golaszewska, H | 1 |
| Lowey, S; Tao, T; Wolff-Long, VL | 1 |
| Flint, DH | 1 |
| Hult, T; Lindberg, U; Strzelecka-Golaszewska, H; Wozniak, A | 1 |
| Beltrán, C; Darszon, A; Ferreira, ST; Garzón-Rodríguez, W; Gómez-Puyou, A; Sepúlveda-Becerra, MA; Strasser, RJ | 1 |
| Muhlrad, A; Peyser, YM; Phan, BC; Reisler, E | 1 |
| Graceffa, P | 1 |
| Branchini, BR; Hinz, LK; Magnasco, N; Magyar, RA; Murtiashaw, MH; Stroh, JG | 1 |
| dos Remedios, CG; Moens, PD | 1 |
| Benkovic, SJ; Sexton, DJ; Soumillion, P | 1 |
| Bhakdi, S; Freytag, C; Harris, R; Kehoe, M; Palmer, M; Tranum-Jensen, J | 1 |
| Hild, G; Lakos, Z; Nyitrai, M; Somogyi, B | 1 |
| Eto, M; Hiratsuka, Y; Morita, F; Yazawa, M | 1 |
| Cramer, WA; Lindeberg, M; Zakharov, SD | 1 |
| Eli-Berchoer, L; Muhlrad, A; Reisler, E | 1 |
| Hemminga, MA; Meijer, AB; Spruijt, RB; Wolfs, CJ | 1 |
| Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S | 1 |
| Hao, Q; Hong, SH; Maret, W | 1 |
| Clements, A; Johnston, MV; Larsen, BS; McEwen, CN | 1 |
| Krishnamoorthy, G; Mukhopadhyay, S; Nayak, PK; Udgaonkar, JB | 1 |
| Liebler, DC; Orton, CR | 1 |
| Bouhallab, S; Brodkorb, A; Croguennec, T; Famelart, MH; Kehoe, JJ; Mollé, D; Morris, ER; Yokoyama, E | 1 |
| Malaga, F; Mayberry, O; Park, DJ; Rodgers, ME; Schleif, RF; Toptygin, D | 1 |
| Jha, SK; Mishra, P | 1 |
53 other study(ies) available for cysteine and 1,5-i-aedans
| Article | Year |
|---|---|
Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP.
Topics: Amino Acid Sequence; Animals; Brain Chemistry; Cattle; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Fatty Acids; Fluorescent Dyes; Lipid Bilayers; Membrane Proteins; Molecular Sequence Data; Myelin Proteins; Myelin Proteolipid Protein; Naphthalenesulfonates; Protein Conformation | 1992 |
Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer.
Topics: Amino Acid Sequence; Cysteine; Energy Transfer; Escherichia coli; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Lysine; Mathematics; Micrococcal Nuclease; Mutagenesis, Site-Directed; Naphthalenesulfonates; Protein Denaturation; Recombinant Proteins; Tryptophan | 1992 |
ATP-dependent Saccharomyces cerevisiae phospho enol pyruvate carboxykinase: isolation and sequence of a peptide containing a highly reactive cysteine.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Cysteine; Escherichia coli; Fluorescent Dyes; Kinetics; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Peptide Fragments; Phosphoenolpyruvate Carboxykinase (GTP); Rats; Saccharomyces cerevisiae; Sequence Homology, Nucleic Acid; Spectrometry, Fluorescence; Trypanosoma brucei brucei | 1992 |
Studies of ligand binding to Escherichia coli adenylosuccinate synthetase.
Topics: Adenosine Monophosphate; Adenylosuccinate Synthase; Binding Sites; Cysteine; Escherichia coli; Fluorescent Dyes; Guanosine Triphosphate; Inosine Monophosphate; Kinetics; Ligands; Naphthalenesulfonates; Protein Conformation; Rhodamines; Spectrometry, Fluorescence | 1991 |
Identification of the reactive cysteinyl residue and ATP binding site in Bacillus cereus glutamine synthetase by chemical modification.
Topics: Adenosine; Adenosine Triphosphate; Amino Acid Sequence; Bacillus cereus; Binding Sites; Cysteine; Fatty Acid Desaturases; Glutamate-Ammonia Ligase; Magnesium; Manganese; Molecular Sequence Data; Naphthalenesulfonates; Oxidoreductases Acting on CH-CH Group Donors | 1990 |
Fluorescence energy transfer distance measurements using site-directed single cysteine mutants. The membrane insertion of colicin A.
Topics: Colicins; Cysteine; Energy Transfer; Fluorescent Dyes; Lipid Bilayers; Models, Chemical; Mutagenesis, Site-Directed; Naphthalenesulfonates; Phosphatidylglycerols; Solubility; Spectrometry, Fluorescence; X-Ray Diffraction | 1991 |
Xenopus transcription factor IIIA. Evidence for heterogeneity of Zn2+ binding affinities and specific labeling of cysteine 287.
Topics: Animals; Binding Sites; Chromatography, Ion Exchange; Cysteine; Dithionitrobenzoic Acid; DNA-Binding Proteins; Female; Fluorescent Dyes; Kinetics; Metalloproteins; Molecular Weight; Naphthalenesulfonates; Ovary; Resorcinols; Transcription Factor TFIIIA; Transcription Factors; Xenopus laevis; Zinc | 1990 |
Fluorescent modification of the cysteine 202 residue of Escherichia coli transcription termination factor rho.
Topics: Adenosine Triphosphatases; Chemical Phenomena; Chemistry; Cross-Linking Reagents; Cysteine; Energy Transfer; Escherichia coli; Fluoresceins; Fluorescent Dyes; Macromolecular Substances; Naphthalenesulfonates; Rho Factor; RNA; Spectrophotometry; Sulfhydryl Reagents; Transcription Factors; Transcription, Genetic | 1988 |
Serine to cysteine mutations in trp repressor protein alter tryptophan and operator binding.
Topics: Amino Acid Sequence; Anilino Naphthalenesulfonates; Bacterial Proteins; Binding Sites; Cysteine; Disulfides; DNA; Fluorescent Dyes; Molecular Sequence Data; Mutation; Naphthalenesulfonates; Operator Regions, Genetic; Repressor Proteins; Serine; Transcription Factors; Tryptophan | 1989 |
Histochemical localization of cysteine-rich proteins by tissue printing on nitrocellulose.
Topics: Antimicrobial Cationic Peptides; Collodion; Cysteine; Histocytochemistry; Hordeum; Lectins; Membranes, Artificial; Naphthalenesulfonates; Oxidation-Reduction; Plant Lectins; Plant Proteins; Proteins; Solanum tuberosum | 1989 |
Fluorescent derivative of cysteine-10 reveals thyroxine-dependent conformational modifications in human serum prealbumin.
Topics: Binding Sites; Binding, Competitive; Cysteine; Fluorescence Polarization; Fluorescent Dyes; Humans; Naphthalenesulfonates; Prealbumin; Protein Conformation; Thyroxine | 1989 |
Fluorescence energy transfer between Cys-10 residues in F-actin filaments.
Topics: Actins; Animals; Cysteine; Energy Transfer; Ethylmaleimide; Fluorescent Dyes; Macromolecular Substances; Muscles; Naphthalenesulfonates; p-Dimethylaminoazobenzene; Rabbits; Spectrometry, Fluorescence; Spectrophotometry | 1986 |
Spectroscopic studies on the riboflavin-sensitized conformational changes of calf lens alpha-crystallin.
Topics: Animals; Cattle; Crystallins; Cysteine; Light; Molecular Weight; Naphthalenesulfonates; Oxidation-Reduction; Photolysis; Protein Conformation; Riboflavin; Spectrometry, Fluorescence; Tryptophan | 1988 |
Fluorescent labeling of cysteinyl residues to facilitate electrophoretic isolation of proteins suitable for amino-terminal sequence analysis.
Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Electrophoresis, Polyacrylamide Gel; Fluoresceins; Fluorescence; Naphthalenesulfonates; Proteins; Serum Albumin, Bovine; Sodium Dodecyl Sulfate | 1987 |
The distance separating Cys-10 from the high-affinity metal binding site in actin.
Topics: Actins; Binding Sites; Cobalt; Cysteine; Fluorescent Dyes; Kinetics; Naphthalenesulfonates; Protein Binding; Protein Conformation; Spectrometry, Fluorescence | 1986 |
Fluorescence energy transfer between points in G-actin: the nucleotide-binding site, the metal-binding site and Cys-373 residue.
Topics: Actins; Adenosine Triphosphate; Animals; Binding Sites; Calcium; Cations, Divalent; Chemical Phenomena; Chemistry, Physical; Cobalt; Cysteine; Energy Transfer; Ethenoadenosine Triphosphate; Fluorescent Dyes; Naphthalenesulfonates; Nickel; Rabbits; Spectrometry, Fluorescence | 1985 |
Distance measurement between the active site and cysteine-177 of the alkali one light chain of subfragment 1 from rabbit skeletal muscle.
Topics: Adenosine Triphosphatases; Animals; Binding Sites; Ca(2+) Mg(2+)-ATPase; Chromatography, High Pressure Liquid; Cysteine; Energy Transfer; Muscles; Myosin Subfragments; Myosins; Naphthalenesulfonates; Peptide Fragments; Rabbits; Trypsin | 1983 |
lac Repressor cysteine-140 reacts selectively with a fluorescent probe bound to the core-headpiece interface.
Topics: Cysteine; Escherichia coli; Iodoacetamide; Naphthalenesulfonates; Repressor Proteins; Transcription Factors; Trypsin | 1984 |
Proximity of reactive cysteine residue and flavin in Escherichia coli pyruvate oxidase as estimated by fluorescence energy transfer.
Topics: Anilino Naphthalenesulfonates; Chemical Phenomena; Chemistry, Physical; Cysteine; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Naphthalenesulfonates; Pyruvate Oxidase; Spectrometry, Fluorescence; Thiamine Pyrophosphate | 1982 |
Use of fluorescence resonance energy transfer to estimate intramolecular distances in the Msx-1 homeodomain.
Topics: Amino Acid Sequence; Chemical Phenomena; Chemistry, Physical; Cysteine; Energy Transfer; Fluorescence; Fluorescent Dyes; Homeodomain Proteins; Models, Molecular; Molecular Sequence Data; MSX1 Transcription Factor; Mutagenesis, Site-Directed; Naphthalenesulfonates; Protein Structure, Secondary; Spectrometry, Fluorescence; Transcription Factors; Tryptophan | 1995 |
Conformational stability of Cys45-alkylated and hydrogen peroxide-oxidised glutathione S-transferase.
Topics: Alkylation; Animals; Cysteine; Dithiothreitol; Enzyme Stability; Glutathione; Glutathione Transferase; Guanidine; Guanidines; Hydrogen Peroxide; Naphthalenesulfonates; Oxidation-Reduction; Protein Conformation; Spectrometry, Fluorescence; Structure-Activity Relationship; Swine; Thermodynamics | 1995 |
Human alpha 2-macroglobulin structure. Location of Cys-949 residues within a half-molecule measured by fluorescence energy transfer.
Topics: alpha-Macroglobulins; Amino Acid Sequence; Cysteine; Energy Transfer; Fluorescent Dyes; Humans; Kinetics; Naphthalenesulfonates; Spectrometry, Fluorescence | 1993 |
Identification of the reactive sulfhydryl group of 1-aminocyclopropane-1-carboxylate deaminase.
Topics: Alanine; Amino Acid Sequence; Amino Acids; Amino Acids, Cyclic; Carbon-Carbon Lyases; Cysteine; Iodoacetamide; Lyases; Molecular Sequence Data; Naphthalenesulfonates; Protein Conformation; Pseudomonas; Spectrophotometry, Ultraviolet; Temperature | 1993 |
C-terminus on actin: spectroscopic and immunochemical examination of its role in actomyosin interactions.
Topics: Actins; Actomyosin; Animals; Aziridines; Cysteine; Dansyl Compounds; Fluorescein; Fluoresceins; Fluorescent Dyes; Immunoglobulin G; Myosin Subfragments; Naphthalenesulfonates; Peptide Fragments; Rabbits; Spectrometry, Fluorescence | 1994 |
Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly.
Topics: Actins; Amino Acid Sequence; Animals; Cysteine; Electrophoresis, Polyacrylamide Gel; Energy Transfer; Fluoresceins; Fluorescent Dyes; Models, Chemical; Molecular Sequence Data; Muscle, Skeletal; Naphthalenesulfonates; Phalloidine; Polymers; Rabbits; Reference Standards; Spectrometry, Fluorescence; Sulfhydryl Reagents | 1994 |
Resonance energy transfer determination of the distance between the four cysteine-364 residues in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase.
Topics: Amino Acid Sequence; Binding Sites; Chemical Phenomena; Chemistry, Physical; Cross-Linking Reagents; Cysteine; Energy Transfer; Fluoresceins; Fluorescent Dyes; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Oxadiazoles; Phosphoenolpyruvate Carboxykinase (GTP); Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Reagents | 1994 |
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product.
Topics: Allylglycine; Azotobacter vinelandii; Bacterial Proteins; Base Sequence; Catalysis; Cysteine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Nitrogenase; Pyridoxal Phosphate; Sulfur | 1994 |
Tryptophan mutants of human C5a anaphylatoxin: a fluorescence anisotropy decay and energy transfer study.
Topics: Amino Acid Sequence; Anaphylatoxins; Circular Dichroism; Complement C5a; Cysteine; Energy Transfer; Fluorescence Polarization; Fluorescent Dyes; Humans; Molecular Sequence Data; Mutation; Naphthalenesulfonates; Recombinant Proteins; Spectrophotometry, Ultraviolet; Sulfhydryl Reagents; Time Factors; Tryptophan | 1993 |
Intermediate conformational states of apocytochrome c.
Topics: Apoproteins; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochromes c; Energy Transfer; Fluorescent Dyes; Hydrochloric Acid; Hydrogen-Ion Concentration; Naphthalenesulfonates; Osmolar Concentration; Perchlorates; Protein Conformation; Protein Folding; Protein Structure, Secondary; Scattering, Radiation; Spectrometry, Fluorescence; X-Rays | 1993 |
Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions.
Topics: Actins; Adenosine Triphosphate; Animals; Cysteine; Fluorescent Dyes; Macromolecular Substances; Magnesium; Naphthalenesulfonates; Peptide Fragments; Potassium Chloride; Protein Conformation; Rabbits; Scattering, Radiation; Spectrometry, Fluorescence; Sulfhydryl Reagents; Trypsin | 1993 |
Proximity relationships between engineered cysteine residues in chicken skeletal myosin regulatory light chain. A resonance energy transfer study.
Topics: Animals; Bone and Bones; Chickens; Cysteine; Energy Transfer; Fluorescence Polarization; Fluorescent Dyes; Maleimides; Molecular Probes; Mutation; Myosin Light Chains; Naphthalenesulfonates | 1995 |
Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase.
Topics: Alanine; Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Disulfides; Escherichia coli; Genes, Bacterial; Haemophilus influenzae; Hydro-Lyases; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Pantetheine; Peptide Fragments; Pyridoxal Phosphate; Sequence Homology, Amino Acid; Sulfhydryl Reagents | 1996 |
Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin.
Topics: Actins; Amino Acid Sequence; Animals; Binding Sites; Calcium; Cations, Divalent; Cysteine; Fluorescent Dyes; Lysine; Macromolecular Substances; Magnesium; Molecular Sequence Data; Muscle, Skeletal; Naphthalenesulfonates; Peptide Fragments; Peptide Mapping; Protein Conformation; Rabbits; Solutions; Subtilisins; Trypsin | 1996 |
Refolding of triosephosphate isomerase in low-water media investigated by fluorescence resonance energy transfer.
Topics: Animals; Cetrimonium; Cetrimonium Compounds; Cysteine; Detergents; Fluorescein-5-isothiocyanate; Guanidine; Guanidines; Hexanols; Micelles; Muscle, Skeletal; Naphthalenesulfonates; Octanes; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Triose-Phosphate Isomerase | 1996 |
Effect of complexes of ADP and phosphate analogs on the conformation of the Cys707-Cys697 region of myosin subfragment 1.
Topics: Adenosine Diphosphate; Animals; Binding Sites; Coumarins; Cysteine; Fluorescent Dyes; Myosin Subfragments; Naphthalenesulfonates; Phosphates; Protein Conformation; Rabbits; Sulfhydryl Reagents | 1997 |
Arrangement of the COOH-terminal and NH2-terminal domains of caldesmon bound to actin.
Topics: 2-Naphthylamine; Actins; Calmodulin-Binding Proteins; Coumarins; Cysteine; Fluorescent Dyes; Kinetics; Maleimides; Muscle, Smooth; Naphthalenesulfonates; Protein Binding; Spectrometry, Fluorescence; Sulfhydryl Reagents; Tropomyosin | 1997 |
Inactivation of firefly luciferase with N-(iodoacetyl)-N'- (5-sulfo-1-naphthyl)ethylenediamine (I-AEDANS).
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Coleoptera; Cysteine; Enzyme Inhibitors; Firefly Luciferin; Luciferases; Molecular Sequence Data; Naphthalenesulfonates; Peptide Mapping; Structure-Activity Relationship; Sulfhydryl Reagents; Trypsin | 1997 |
A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374.
Topics: Actins; Animals; Computer Simulation; Cysteine; Energy Transfer; Fluorescence; Fluorescent Dyes; Models, Molecular; Myosins; Naphthalenesulfonates; Protein Conformation; Rabbits; Spectrometry, Fluorescence | 1997 |
Clamp subunit dissociation dictates bacteriophage T4 DNA polymerase holoenzyme disassembly.
Topics: Bacteriophage T4; Coenzymes; Cysteine; DNA-Directed DNA Polymerase; Kinetics; Mutagenesis, Site-Directed; Naphthalenesulfonates; Spectrometry, Fluorescence; Trans-Activators; Tryptophan; Valine; Viral Proteins | 1998 |
Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.
Topics: Animals; Bacterial Proteins; Cell Membrane Permeability; Complement Hemolytic Activity Assay; Cysteine; Erythrocyte Membrane; Membrane Lipids; Mutation; Naphthalenesulfonates; Protein Conformation; Rabbits; Streptolysins | 1998 |
Effect of Ca2+-Mg2+ exchange on the flexibility and/or conformation of the small domain in monomeric actin.
Topics: Actins; Animals; Calcium; Calibration; Cysteine; Energy Transfer; Fluorescent Dyes; Lysine; Magnesium; Models, Molecular; Muscle, Skeletal; Naphthalenesulfonates; Protein Conformation; Rabbits; Spectrometry, Fluorescence | 1998 |
Reactivities of Cys707 (SH1) in intermediate states of myosin subfragment-1 ATPase.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Cysteine; Fluorescent Dyes; Myosins; Naphthalenesulfonates; Protein Conformation; Rabbits | 1998 |
Kinetic description of structural changes linked to membrane import of the colicin E1 channel protein.
Topics: Biological Transport; Cell Membrane; Circular Dichroism; Colicins; Cysteine; Energy Transfer; Ion Channels; Kinetics; Lipid Bilayers; Models, Chemical; Naphthalenesulfonates; Peptide Fragments; Phosphatidylcholines; Phosphatidylethanolamines; Protein Precursors; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan | 1999 |
Structural implications of the chemical modification of Cys(10) on actin.
Topics: Actins; Amino Acid Sequence; Animals; Binding Sites; Cysteine; Fluorescent Dyes; Macromolecular Substances; Microfilament Proteins; Models, Molecular; Muscle, Skeletal; Myosin Subfragments; Myosins; Naphthalenesulfonates; Protein Structure, Secondary; Rabbits; Spectrometry, Fluorescence | 2000 |
Configurations of the N-terminal amphipathic domain of the membrane-bound M13 major coat protein.
Topics: Amino Acid Sequence; Bacteriophage M13; Capsid; Capsid Proteins; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Fluorescent Dyes; Membrane Proteins; Membranes, Artificial; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Peptide Fragments; Phosphatidylcholines; Protein Binding; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spin Labels | 2001 |
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
Topics: Aldehyde Oxidase; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Cysteine; Cytosol; Fluorescent Dyes; Genetic Vectors; Iron-Sulfur Proteins; Kinetics; Lyases; Lysine; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Naphthalenesulfonates; Pichia; Plant Proteins; Protein Binding; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Selenocysteine; Spectrophotometry; Substrate Specificity; Sulfides; Sulfurtransferases; Xanthine Dehydrogenase | 2005 |
Domain-specific fluorescence resonance energy transfer (FRET) sensors of metallothionein/thionein.
Topics: Biosensing Techniques; Cysteine; Ergothioneine; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Humans; Metallothionein; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Naphthalenesulfonates; Protein Conformation; Protein Isoforms; Recombinant Proteins; Sulfhydryl Reagents; Tryptophan; Zinc | 2005 |
Fluorescence-based peptide labeling and fractionation strategies for analysis of cysteine-containing peptides.
Topics: Affinity Labels; Chemical Fractionation; Cysteine; Fluorescence; Molecular Structure; Naphthalenesulfonates; Peptides | 2005 |
Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics.
Topics: Amyloid; Bacillus; Bacterial Proteins; Cysteine; Fluorescence Polarization; Fluorescent Dyes; Microscopy, Atomic Force; Models, Molecular; Mutagenesis, Site-Directed; Naphthalenesulfonates; Protein Structure, Quaternary; Thermodynamics | 2006 |
Analysis of protein adduction kinetics by quantitative mass spectrometry: competing adduction reactions of glutathione-S-transferase P1-1 with electrophiles.
Topics: Biotin; Cysteine; Glutathione S-Transferase pi; Isocyanates; Kinetics; Naphthalenesulfonates; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Mass Spectrometry | 2007 |
Determination of exposed sulfhydryl groups in heated beta-lactoglobulin A using IAEDANS and mass spectrometry.
Topics: Cysteine; Hot Temperature; Lactoglobulins; Naphthalenesulfonates; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Compounds; Sulfhydryl Reagents | 2007 |
A genetic and physical study of the interdomain linker of E. Coli AraC protein--a trans-subunit communication pathway.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arabinose; AraC Transcription Factor; Cysteine; Escherichia coli; Escherichia coli Proteins; Fluorescence Polarization; Gene Expression; Mutation; Naphthalenesulfonates; Proline; Protein Binding; Protein Domains; Protein Folding; Protein Multimerization; Protein Subunits; Recombinant Proteins; Spectrometry, Fluorescence; Thermodynamics | 2016 |
Slow Motion Protein Dance Visualized Using Red-Edge Excitation Shift of a Buried Fluorophore.
Topics: Cysteine; Fluorescent Dyes; Humans; Naphthalenesulfonates; Protein Conformation, alpha-Helical; Protein Structure, Tertiary; Protein Unfolding; Serum Albumin, Human; Spectrometry, Fluorescence | 2019 |