tryptophan has been researched along with cytochrome c-t in 48 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (12.50) | 18.7374 |
| 1990's | 9 (18.75) | 18.2507 |
| 2000's | 18 (37.50) | 29.6817 |
| 2010's | 13 (27.08) | 24.3611 |
| 2020's | 2 (4.17) | 2.80 |
| Authors | Studies |
|---|---|
| Acharya, AS; Iyer, KS; Khandke, KM; Manjula, BN; Sahni, G | 1 |
| Gallay, J; Vincent, M | 1 |
| Davies, AM; Greenwood, C; Guillemette, JG; Mauk, AG; Moore, GR; Smith, M; Thurgood, AG | 1 |
| Brochon, JC; Gallay, J; Jordi, W; Merola, F; Vincent, M | 1 |
| Berkhout, TA; de Kruijff, B; Marsh, D; Rietveld, A; Roenhorst, A | 1 |
| Berkhout, TA; de Kruijff, B; Rietveld, A | 1 |
| Mataga, N; Tanaka, F | 1 |
| Borchart, U; Machleidt, W; Schägger, H; von Jagow, G | 1 |
| Erman, JE; Miller, MA; Vitello, L | 1 |
| Han, X; Tong, J; Yang, F | 1 |
| Bowler, BE; Dong, A; Garbin, K; Godbole, S | 1 |
| Pinheiro, TJ; Rankin, SE; Watts, A | 1 |
| Pinheiro, TJ; Rankin, SE; Roder, H; Watts, A | 1 |
| Bryson, EA; Carey, M; Pinheiro, TJ; Rankin, SE; Watts, A | 1 |
| Döpner, S; Harris, TR; Hildebrand, DP; Hildebrandt, P; Mauk, AG; Rosell, FI | 1 |
| Ahuja, U; Ren, Q; Thöny-Meyer, L | 1 |
| Bowler, BE; Smith, CR; Wandschneider, E | 1 |
| Chen, SM; Huang, ZX; Li, LZ; Song, AX; Yu, T | 1 |
| KREIL, G | 1 |
| Ahuja, U; Thöny-Meyer, L | 1 |
| Oldfield, E; Sun, H | 1 |
| Cherepanov, AV; de Vries, S; Ludwig, B; MacMillan, F; Richter, OM; Wiertz, FG | 1 |
| Hynek, R; Kodícek, M; Santrůcek, J; Strohalm, M | 1 |
| Rousseau, DL; Yeh, SR; Zhong, S | 1 |
| Bo, T; Pawliszyn, J | 1 |
| Basova, LV; Belikova, NA; Kagan, VE; Kapralov, AA; Kurnikov, IV; Osipov, AN; Peterson, J; Potapovich, MV; Tyurin, VA; Vladimirov, YA | 1 |
| Basova, LV; Bayir, H; Belikova, NA; Jiang, J; Kagan, VE; Kapralov, AA; Kurnikov, IV; Tyurin, VA; Tyurina, YY; Vladimirov, YA; Vlasova, II; Zhao, Q | 1 |
| Anderson, VE; Guo, M; Kenney, ME; Kim, J; Oleinick, NL; Rodriguez, ME | 1 |
| Adak, S; Dolai, S; Pal, S; Yadav, RK | 1 |
| Shibayama, N | 1 |
| Cársky, J; Labieniec, M; Malinska, D; Przygodzki, T; Rysz, J; Watala, C | 1 |
| Guo, L; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Barros, MP; Bechara, EJ; Dyszy, FH; Faria, PA; Mano, CM; Nantes, IL; Nascimento, OR; Prieto, T | 1 |
| Bräm, O; Cannizzo, A; Chergui, M; Consani, C | 1 |
| Amani, S; Naeem, A | 1 |
| Didik, J; Domazou, AS; Gebicka, L; Gebicki, JL; Koppenol, WH; van der Meijden, B | 1 |
| Landahl, EC; Rice, SE | 1 |
| Fitzgerald, MC; Strickland, EC; Xu, Y | 1 |
| Friedlander, RM; Jiang, J; Li, W; Mao, LL; Sirianni, AC; Sugarbaker, P; Wang, X; Zeng, J; Zhang, X; Zhou, S | 1 |
| Chen, F; Luo, Y; Pu, X; Qu, X; Yang, L; Yang, Y; Zhang, G | 1 |
| Louder, A; Meints, CE; Mothersole, RG; Wolthers, KR | 1 |
| Baldini, E; Bauer, B; Chergui, M; Mewes, L; Nagornova, NS; Oppermann, M; Oriana, A; Palmieri, T; Rossi, T; van Mourik, F | 1 |
| Attar, F; Falahati, M; Mansouri, A; Mousavi, M; Saboury, AA | 1 |
| Bowler, BE; Elmer-Dixon, MM | 1 |
| Agarwal, MC; Garg, M; Kumar, R; Kumar, V; Sharma, D | 1 |
| Padmanabhan, B; Srinivas Bharath, MM; Thiyagarajan, S; Unni, S | 1 |
| He, ZW; Jin, HY; Li, Z; Liu, W; Ren, YX; Sun, Q; Tang, CC; Wang, A; Zhou, AJ | 1 |
| Arrell, CA; Bacellar, C; Biednov, M; Bressler, C; Cannelli, O; Chergui, M; Cirelli, C; Gawelda, W; Ingle, RA; Johnson, PJM; Khakhulin, D; Kinschel, D; Knopp, G; Kubicek, K; Lima, FA; Mancini, GF; Menzi, S; Milne, CJ; Ozerov, D; Pamfilidis, G; Rodriguez-Fernandez, A; Rouxel, JR; Szlachetko, J; Zhao, Y | 1 |
48 other study(ies) available for tryptophan and cytochrome c-t
| Article | Year |
|---|---|
Restriction in the conformational flexibility of apoproteins in the presence of organic cosolvents: a consequence of the formation of "native-like conformation".
Topics: 1-Propanol; Antigens, Bacterial; Apoproteins; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carrier Proteins; Cytochrome c Group; Cytochromes c; Globins; Hydrogen-Ion Concentration; Protein Conformation; Protein Structure, Secondary; Ribonuclease, Pancreatic; Serine Endopeptidases; Solvents; Spectrometry, Fluorescence; Temperature; Trypsin; Tryptophan | 1992 |
The interactions of horse heart apocytochrome c with phospholipid vesicles and surfactant micelles: time-resolved fluorescence study of the single tryptophan residue (Trp-59).
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Fluorescence Polarization; Horses; In Vitro Techniques; Liposomes; Micelles; Myocardium; Phospholipids; Protein Binding; Surface-Active Agents; Tryptophan | 1991 |
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
Topics: Amino Acids; Cytochrome c Group; Cytochromes c; Heme; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Tryptophan; Tyrosine | 1991 |
Nanosecond dynamics of horse heart apocytochrome c in aqueous solution as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59).
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Fluorescence Polarization; Horses; Kinetics; Mathematics; Models, Theoretical; Myocardium; Protein Conformation; Solutions; Time Factors; Tryptophan | 1988 |
Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes.
Topics: Apoproteins; Biological Transport; Cytochrome c Group; Cytochromes c; Electron Spin Resonance Spectroscopy; Energy Transfer; In Vitro Techniques; Membrane Fluidity; Membrane Lipids; Phosphatidylcholines; Phosphatidylglycerols; Phosphatidylserines; Phospholipids; Spectrometry, Fluorescence; Tryptophan | 1986 |
Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids.
Topics: Apoproteins; Bromine; Cytochrome c Group; Cytochromes c; Membranes, Artificial; Phosphatidylcholines; Phosphatidylserines; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 1987 |
Fluorescence quenching dynamics of tryptophan in proteins. Effect of internal rotation under potential barrier.
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Electron Transport Complex IV; Fluorescence Polarization; Horses; Kinetics; Mathematics; Models, Theoretical; Myocardium; Proteins; Tryptophan | 1987 |
Amino-acid sequence of the smallest protein of the cytochrome c1 subcomplex from beef heart mitochondria.
Topics: Amino Acid Sequence; Animals; Cattle; Cytochrome c Group; Cytochromes c; Cytochromes c1; Mitochondria, Heart; Tryptophan | 1983 |
Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase.
Topics: Animals; Cytochrome c Group; Cytochrome-c Peroxidase; Cytochromes c; Electron Transport; Escherichia coli; Horses; In Vitro Techniques; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity; Tryptophan | 1995 |
Further study on the spontaneous partial folding of chicken heart apocytochrome c.
Topics: Animals; Apoproteins; Chickens; Cytochrome c Group; Cytochromes c; Fluorescence Polarization; Myocardium; Protein Folding; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Surface Properties; Tryptophan | 1994 |
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.
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 |
Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid.
Topics: Animals; Apoproteins; Circular Dichroism; Cytochrome c Group; Cytochromes c; Horses; Phosphatidylglycerols; Phospholipids; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Static Electricity; Tryptophan | 1998 |
Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state.
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Horses; Hydrogen-Ion Concentration; Iodine; Kinetics; Lipids; Lysophospholipids; Micelles; Myocardium; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan | 1999 |
Folding of apocytochrome c in lipid micelles: formation of alpha-helix precedes membrane insertion.
Topics: Animals; Apoproteins; Binding Sites; Circular Dichroism; Cytochrome c Group; Cytochromes c; Horses; Kinetics; Lipid Bilayers; Lysophosphatidylcholines; Micelles; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan | 1999 |
Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Enzyme Stability; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Structure-Activity Relationship; Tryptophan | 2000 |
A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.
Topics: Amino Acid Motifs; Amino Acid Sequence; Apoproteins; Bacterial Outer Membrane Proteins; Cytochrome c Group; Cytochromes c; DNA Primers; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Lyases; Models, Biological; Molecular Sequence Data; Mutation; Periplasm; Plasmids; Point Mutation; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Protein Transport; Tryptophan | 2002 |
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.
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 |
Role of tryptophan 121 in the soluble CuA domain of cytochrome c oxidase: structure and electron transfer studies.
Topics: Animals; Copper; Cytochromes c; Electron Transport; Electron Transport Complex IV; Electrons; Escherichia coli; Horses; Mutagenesis, Site-Directed; Mutation; Paracoccus; Structure-Activity Relationship; Tryptophan | 2003 |
[ON SPECIES SPECIFICITY OF CYTOCHROME C: COMPARISON OF THE AMINO ACID SEQUENCE OF TUNA FISH CYTOCHROME C WITH HORSE CYTOCHROME C].
Topics: Amino Acid Sequence; Amino Acids; Animals; Chemical Phenomena; Chemistry; Chromatography; Cytochromes; Cytochromes c; Fishes; Histidine; Horses; Peptides; Research; Species Specificity; Tryptophan; Tuna | 1963 |
Dynamic features of a heme delivery system for cytochrome C maturation.
Topics: Alanine; Amino Acid Motifs; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Division; Cytochromes c; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Hemeproteins; Histidine; Membrane Proteins; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Periplasm; Phenotype; Plasmids; Precipitin Tests; Protein Binding; Subcellular Fractions; Tryptophan | 2003 |
Tryptophan chemical shift in peptides and proteins: a solid state carbon-13 nuclear magnetic resonance spectroscopic and quantum chemical investigation.
Topics: Animals; Carbon Isotopes; Carboxyhemoglobin; Chickens; Cytochromes c; Egg Proteins; Horses; Models, Molecular; Muramidase; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Proteins; Quantum Theory; Tryptophan | 2004 |
An oxo-ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxidases trapped by microsecond freeze-hyperquenching (MHQ).
Topics: Bacterial Proteins; Cytochromes c; Electron Spin Resonance Spectroscopy; Escherichia coli; Freezing; Oxidation-Reduction; Oxidoreductases; Oxygen; Paracoccus denitrificans; Tryptophan | 2004 |
Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry.
Topics: 2-Hydroxy-5-nitrobenzyl Bromide; Animals; Binding Sites; Cattle; Cytochromes c; Horses; Humans; Muramidase; Myoglobin; Protein Binding; Serum Albumin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tryptophan | 2004 |
Modulation of the folding energy landscape of cytochrome C with salt.
Topics: Cytochromes c; Fluorescence; Heme; Kinetics; Potassium Chloride; Protein Folding; Thermodynamics; Tryptophan | 2004 |
Characterization of bovine serum albumin-tryptophan interaction by capillary isoelectric focusing with whole column imaging detection.
Topics: Animals; Binding Sites; Cattle; Cytochromes c; Electrophoresis, Capillary; Isoelectric Focusing; Protein Binding; Serum Albumin, Bovine; Stereoisomerism; Tryptophan | 2006 |
Peroxidase activity and structural transitions of cytochrome c bound to cardiolipin-containing membranes.
Topics: Acridine Orange; Animals; Binding, Competitive; Cardiolipins; Cell Membrane; Cytochromes c; Electrophoresis; Enzyme Activation; Etoposide; Fluoresceins; Horses; Hydrophobic and Hydrophilic Interactions; Lipids; Liposomes; Osmolar Concentration; Oxidation-Reduction; Peroxidase; Phosphatidylcholines; Spectrometry, Fluorescence; Structure-Activity Relationship; Time Factors; Tryptophan | 2006 |
The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Activation; Etoposide; Fluorescence; Heme; Humans; Mice; Peroxidase; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Phosphates; Phosphatidylserines; Phospholipids; Protein Structure, Tertiary; Tryptophan | 2007 |
Oxidative modification of cytochrome c by singlet oxygen.
Topics: Animals; Apoptosis; Cytochromes c; Histidine; Horses; Hydrogen-Ion Concentration; Methionine; Mitochondria; Models, Biological; Models, Chemical; Myocardium; Oxygen; Photochemotherapy; Reactive Oxygen Species; Tryptophan | 2008 |
Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme.
Topics: Amino Acid Sequence; Animals; Ascorbate Peroxidases; Ascorbic Acid; Cytochromes c; Hydrogen Peroxide; Kinetics; Leishmania major; Models, Biological; Molecular Sequence Data; Mutant Proteins; Oxidation-Reduction; Peroxidases; Phenylalanine; Spectrum Analysis; Structure-Activity Relationship; Substrate Specificity; Tryptophan | 2008 |
Slow motion analysis of protein folding intermediates within wet silica gels.
Topics: Animals; Biochemistry; Circular Dichroism; Cytochromes c; Gels; Horses; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Silicon Dioxide; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan | 2008 |
Effects of resorcylidene aminoguanidine (RAG) on selected parameters of isolated rat liver mitochondria.
Topics: Animals; Calcium; Cytochromes c; Dose-Response Relationship, Drug; Drug Evaluation, Preclinical; Guanidines; Lipid Bilayers; Male; Mitochondria, Liver; Mitochondrial Membranes; Oxygen; Rats; Rats, Wistar; Serum Albumin, Bovine; Tryptophan | 2009 |
Ultrafast proteinquake dynamics in cytochrome c.
Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan | 2009 |
Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Lipid Peroxidation; Nitrosation; Oxidation-Reduction; Oxidative Stress; Peroxidase; Peroxynitrous Acid; Protein Processing, Post-Translational; Protein Structure, Secondary; Spectrophotometry; Superoxides; Tryptophan; Unilamellar Liposomes | 2009 |
Femtosecond UV studies of the electronic relaxation processes in Cytochrome c.
Topics: Animals; Cytochromes c; Electrons; Energy Transfer; Heme; Horses; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Time Factors; Tryptophan | 2011 |
Detection and analysis of amorphous aggregates and fibrils of cytochrome c in the presence of phenolic acids.
Topics: Animals; Antioxidants; Benzothiazoles; Coumaric Acids; Cytochromes c; Fluorescent Dyes; Gallic Acid; Horses; Microscopy, Fluorescence; Multiprotein Complexes; Protein Multimerization; Protein Stability; Protein Structure, Quaternary; Protein Structure, Secondary; Proteostasis Deficiencies; Single-Cell Analysis; Thiazoles; Tryptophan | 2013 |
The kinetics of the reaction of nitrogen dioxide with iron(II)- and iron(III) cytochrome c.
Topics: Amino Acids; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Nitrogen Dioxide; Oxidation-Reduction; Pulse Radiolysis; Tryptophan; Tyrosine | 2014 |
Model-independent decomposition of two-state data.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Kinesins; Models, Molecular; Proteins; Scattering, Small Angle; Spectrometry, Fluorescence; Tryptophan; X-Ray Diffraction | 2013 |
Thermodynamic analysis of protein folding and stability using a tryptophan modification protocol.
Topics: Amino Acid Sequence; Cytochromes c; Methionine; Molecular Sequence Data; Muramidase; Protein Folding; Protein Stability; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfonium Compounds; Thermodynamics; Tryptophan | 2014 |
N-acetyl-l-tryptophan, but not N-acetyl-d-tryptophan, rescues neuronal cell death in models of amyotrophic lateral sclerosis.
Topics: Amyotrophic Lateral Sclerosis; Animals; Apoptosis; Caspases; Cell Line; Cytochromes c; Drug Evaluation, Preclinical; Hybrid Cells; Interleukin-1beta; Mice; Mitochondria; Motor Neurons; Neurokinin-1 Receptor Antagonists; Neuroprotective Agents; Proteasome Endopeptidase Complex; Receptors, Neurokinin-1; Stereoisomerism; Substance P; Tryptophan | 2015 |
Molecular Cloning, Heterologous Expression, and Functional Characterization of an NADPH-Cytochrome P450 Reductase Gene from Camptotheca acuminata, a Camptothecin-Producing Plant.
Topics: Amino Acid Sequence; Antineoplastic Agents; Camptotheca; Camptothecin; Catalysis; Cloning, Molecular; Cytochromes c; DNA, Complementary; Escherichia coli; Gene Expression Regulation, Plant; Models, Molecular; Molecular Conformation; Molecular Sequence Data; NADPH-Ferrihemoprotein Reductase; Open Reading Frames; Phylogeny; Plant Leaves; Plant Roots; Plant Stems; Recombinant Proteins; Sequence Homology, Amino Acid; Tryptophan | 2015 |
Role of active site loop in coenzyme binding and flavin reduction in cytochrome P450 reductase.
Topics: Alanine; Arabidopsis; Arginine; Aspartic Acid; Bacillus megaterium; Catalysis; Catalytic Domain; Chromatography, High Pressure Liquid; Cytochromes c; Flavins; Humans; Hydrogen Bonding; Kinetics; Mutagenesis, Site-Directed; Mutation; NADP; NADPH-Ferrihemoprotein Reductase; Protein Binding; Protein Domains; Saccharomyces cerevisiae; Static Electricity; Tryptophan | 2016 |
The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science.
Topics: Animals; Cytochromes c; Heart; Horses; Myoglobin; Spectrophotometry, Ultraviolet; Time Factors; Tryptophan; Ultraviolet Rays | 2017 |
Interaction of manganese nanoparticle with cytochrome c: A multi-spectroscopic study.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochromes c; Hydrophobic and Hydrophilic Interactions; Manganese; Metal Nanoparticles; Models, Molecular; Particle Size; Phenylalanine; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrum Analysis; Static Electricity; Temperature; Thermodynamics; Tryptophan; Tyrosine | 2018 |
Electrostatic Constituents of the Interaction of Cardiolipin with Site A of Cytochrome c.
Topics: Amino Acid Substitution; Cardiolipins; Cytochromes c; Fluorescence; Lysine; Protein Binding; Protein Conformation; Saccharomyces cerevisiae; Static Electricity; Thermodynamics; Tryptophan | 2018 |
Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.
Topics: Alkalies; Circular Dichroism; Cytochromes c; Dextrans; Ficoll; Hydrogen-Ion Concentration; Molecular Structure; Molecular Weight; Muramidase; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Thermodynamics; Tryptophan | 2018 |
Tryptophan Oxidation in the UQCRC1 Subunit of Mitochondrial Complex III (Ubiquinol-Cytochrome C Reductase) in a Mouse Model of Myodegeneration Causes Large Structural Changes in the Complex: A Molecular Dynamics Simulation Study.
Topics: Animals; Cytochromes c; Electron Transport Complex III; Mice; Molecular Dynamics Simulation; Muscular Diseases; Oxidation-Reduction; Tryptophan | 2019 |
Role of extracellular polymeric substances in methane production from waste activated sludge induced by conductive materials.
Topics: Anaerobiosis; Bioreactors; Carbon; Cytochromes c; Extracellular Polymeric Substance Matrix; Ferrosoferric Oxide; Iron; Methane; Polysaccharides; Sewage; Tryptophan; Tyrosine | 2022 |
Ultrafast Energy Transfer from Photoexcited Tryptophan to the Haem in Cytochrome c.
Topics: Cytochromes c; Electron Transport; Energy Transfer; Heme; Iron; Tryptophan | 2023 |