heme and guanidine
heme has been researched along with guanidine in 67 studies
Research
Studies (67)
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 3 (4.48) | 18.7374 |
1990's | 14 (20.90) | 18.2507 |
2000's | 35 (52.24) | 29.6817 |
2010's | 14 (20.90) | 24.3611 |
2020's | 1 (1.49) | 2.80 |
Authors
Authors | Studies |
---|---|
Fisher, MT | 1 |
Falksen, K; Horowitz, P; Muhoberac, BB; Wharton, DC | 1 |
Bucci, E; Franchi, D; Fronticelli, C | 1 |
Bhuyan, A; Chan, CK; Eaton, WA; Henry, ER; Hofrichter, J; Hu, Y; Jones, CM; Luck, SD; Roder, H | 1 |
Chapman, SK; Coggins, JR; Daff, S; Lindsay, JG; Munro, AW | 1 |
Coggins, JR; Kelly, S; Lindsay, JG; Munro, AW; Price, NC | 1 |
Hargrove, MS; Olson, JS | 1 |
Eaton, WA; Hagen, SJ; Hofrichter, J; Szabo, A | 1 |
MacKenzie, NE; Roder, H; Sauder, JM | 1 |
Yamamoto, Y | 1 |
Chan, CK; Eaton, WA; Hofrichter, J; Hu, Y; Rousseau, DL; Takahashi, S | 1 |
Bowler, BE; Godbole, S; Hammack, B | 2 |
Dutton, PL; Gibney, BR; Rabanal, F; Reddy, KS | 1 |
Wittung-Stafshede, P | 1 |
Bocian, DF; Kalsbeck, WA; Olson, JS; Tang, Q | 1 |
Rousseau, DL; Yeh, SR | 1 |
Chattopadhyay, K; Mazumdar, S | 1 |
Eaton, WA; Hagen, SJ | 1 |
Guidry, J; Moczygemba, C; Wittung-Stafshede, P | 1 |
Ferguson, SJ; Tomlinson, EJ | 2 |
Nall, BT; Pierce, MM | 1 |
Arnesano, F; Banci, L; Bertini, I; Koulougliotis, D; Monti, A | 1 |
Bowler, BE; Nelson, CJ | 1 |
Carswell, CW; Hagen, SJ; Sjolander, EM | 1 |
Abbruzzetti, S; Libertini, LJ; Small, EW; Small, JR; Viappiani, C | 1 |
Banci, L; Bertini, I; Branchini, BR; Hajieva, P; Spyroulias, GA; Turano, P | 1 |
Bowler, BE; Hammack, BN; Smith, CR | 1 |
Bartalesi, I; Bertini, I; Ghosh, K; Rosato, A; Turano, P | 1 |
Bowler, BE; Smith, CR; Wandschneider, E | 1 |
Ascoli, F; Howes, BD; Piro, MC; Santucci, R; Sinibaldi, F; Smulevich, G | 1 |
DANIELI, G; MASETTI, GP; SANGIORGI, F | 1 |
Bowler, BE; Wandschneider, E | 1 |
Ito, A; Kudo, K; Sakamoto, S; Yoshikawa, S | 1 |
Banci, L; Barker, PD; Bruix, M; Ciofi-Baffoni, S; de Lumley Woodyear, T; Fersht, AR; Garcia, P; Johnson, CM; Ramachandra Shastry, MC; Rico, M; Roder, H | 1 |
Canters, GW; Ciofi-Baffoni, S; Diederix, RE; Lowe, CE; Prudêncio, M; Ubbink, M; Worrall, JA | 1 |
Floris, G; Longu, S; Medda, R; Mura, A; Padiglia, A; Rinaldi, AC | 1 |
Ishimori, K; Kimura, T; Morishima, I; Sakamoto, K | 1 |
Boucher, JL; Mansuy, D; Mattioli, TA; Moreau, M; Santolini, J; Stuehr, DJ | 1 |
Halder, P; Hargrove, MS; Hoy, JA; Smagghe, BJ | 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 |
Ascenzi, P; Coletta, M; De Sanctis, G; Fanali, G; Fasano, M; Gioia, 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 |
Gray, HB; Kimura, T; Lee, JC; Winkler, JR | 1 |
Burstyn, JN; Clark, RW; Lee, AJ; Ponter, S; Youn, H | 1 |
Li, X; Lin, Y; Mao, L; Su, L; Yu, P; Zhang, L; Zheng, W | 1 |
Balland, V; Boucher, JL; Giroud, C; Mattioli, TA; Moreau, M; Santolini, J; Stuehr, DJ; Xu-Li, Y | 1 |
Bischin, C; Cooper, CE; Damian, G; Deac, F; Rajagopal, BS; Silaghi-Dumitrescu, R; Worrall, JA | 1 |
Fuchs, MR; He, C; Knipp, M; Ogata, H | 1 |
Bandara, DM; Freeman, TL; Hong, Y; Pletneva, EV; Schiavoni, KH | 1 |
Bowler, BE; Khan, MK | 1 |
Behera, RK; Mazumdar, S; Nakajima, H; Rajbongshi, J; Watanabe, Y | 1 |
Champion, PM; Karunakaran, V; Sun, Y | 1 |
Dong, L; Jurban, BJ; Sharma, NP; Smith, WL | 1 |
Dellarole, M; Guca, E; Roumestand, C; Royer, CA; Vallone, B | 1 |
Choi, J; Fujitsuka, M; Majima, T; Tojo, S | 1 |
Barbero, L; Bojić, M; Dolgos, H; Freisleben, A; Gallemann, D; Guengerich, FP; Riva, S | 1 |
Cha, HJ; Choi, KY; Jang, DS; Jin, KS | 1 |
Olson, JS; Ou, WC; Phillips, GN; Samuel, PP | 1 |
Bowler, BE; Danielson, TA | 1 |
Ahmad, F; Ahmed, A; Hassan, MI; Islam, A; Lakhrm, NA; Malik, A; Nasreen, K; Parray, ZA; Shamsi, A | 1 |
Other Studies
67 other study(ies) available for heme and guanidine
Article | Year |
---|---|
Differences in thermal stability between reduced and oxidized cytochrome b562 from Escherichia coli.
Topics: Cytochrome b Group; Electron Transport; Enzyme Stability; Escherichia coli; Escherichia coli Proteins; Guanidine; Guanidines; Heme; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Spectrophotometry, Ultraviolet; Thermodynamics | 1991 |
Perturbation of Pseudomonas cytochrome oxidase by guanidine hydrochloride to detect differential stabilization of the heme d1 and heme c moieties.
Topics: Chromatography, Gel; Circular Dichroism; Electron Transport Complex IV; Guanidine; Guanidines; Heme; Macromolecular Substances; Pseudomonas; Spectrometry, Fluorescence | 1986 |
Folding domains as functional tools in allosteric systems: a heme-dependent domain in hemoglobin beta subunits.
Topics: Allosteric Site; Guanidine; Guanidines; Heme; Hemoglobins; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Mathematics; Protein Conformation; Temperature; Thermodynamics | 1982 |
Fast events in protein folding initiated by nanosecond laser photolysis.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Guanidine; Guanidines; Heme; Horses; Kinetics; Lasers; Methionine; Photolysis; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrophotometry; Time Factors | 1993 |
Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Guanidine; Guanidines; Heme; Kinetics; Mixed Function Oxygenases; NAD; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Quinones; Spectrophotometry | 1996 |
Deflavination of cytochrome P450 BM3 by treatment with guanidinium chloride.
Topics: Bacillus megaterium; Bacterial Proteins; Circular Dichroism; Cytochrome P-450 Enzyme System; Flavins; Guanidine; Guanidines; Heme; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation | 1996 |
The stability of holomyoglobin is determined by heme affinity.
Topics: Animals; Binding Sites; Circular Dichroism; Fluorescence; Globins; Guanidine; Guanidines; Heme; Iron; Kinetics; Metmyoglobin; Mutagenesis; Myoglobin; Oxidation-Reduction; Protein Binding; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrophotometry; Whales | 1996 |
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.
Topics: Cytochrome c Group; Diffusion; Guanidine; Guanidines; Heme; Kinetics; Ligands; Methionine; Models, Structural; Peroxidases; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry; Time Factors | 1996 |
Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2.
Topics: Cytochrome c Group; Cytochromes c2; Guanidine; Guanidines; Heme; Kinetics; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Rhodobacter capsulatus; Solvents; Thermodynamics | 1996 |
1H-NMR study of inter-segmental hydrogen bonds in sperm whale and horse apomyoglobins.
Topics: Animals; Apoproteins; Aspartic Acid; Guanidine; Guanidines; Heme; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Protein Denaturation; Temperature; Whales | 1997 |
Submillisecond protein folding kinetics studied by ultrarapid mixing.
Topics: Animals; Cytochrome c Group; Fluorescence; Guanidine; Guanidines; Heme; Horses; Imidazoles; Kinetics; Myocardium; Protein Denaturation; Protein Folding; Tryptophan | 1997 |
Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation.
Topics: Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Protein Denaturation; Protein Folding | 1998 |
Effect of four helix bundle topology on heme binding and redox properties.
Topics: Amino Acid Sequence; Carbon Monoxide; Chromatography, Gel; Circular Dichroism; Guanidine; Heme; Hemeproteins; Iron Compounds; Ligands; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Denaturation; Protein Structure, Secondary | 1998 |
A stable, molten-globule-like cytochrome c.
Topics: Circular Dichroism; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Sequence Analysis; Thermus thermophilus; Tryptophan | 1998 |
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
Topics: Acids; Animals; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Male; Mutagenesis, Site-Directed; Myoglobin; Protein Folding; Spectrophotometry; Spermatozoa; Whales | 1998 |
Ligand exchange during unfolding of cytochrome c.
Topics: Animals; Circular Dichroism; Cytochrome c Group; Guanidine; Heme; Horses; Kinetics; Ligands; Myocardium; Protein Denaturation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Thermodynamics; Tryptophan | 1999 |
Structural and conformational stability of horseradish peroxidase: effect of temperature and pH.
Topics: Calcium; Circular Dichroism; Enzyme Stability; Guanidine; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Temperature; Tryptophan | 2000 |
Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
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 |
Two-state expansion and collapse of a polypeptide.
Topics: Animals; Computer Simulation; Cytochrome c Group; Diffusion; Guanidine; Heme; Horses; Kinetics; Lasers; Models, Chemical; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tryptophan; Viscosity | 2000 |
Heme orientation affects holo-myoglobin folding and unfolding kinetics.
Topics: Animals; Apoproteins; Circular Dichroism; Dose-Response Relationship, Drug; Fluorescence; Guanidine; Heme; Horses; Kinetics; Metmyoglobin; Myoglobin; Protein Denaturation; Protein Folding; Protein Renaturation; Rotation; Thermodynamics; Tryptophan; Whales | 2000 |
Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: implications for c type cytochrome biogenesis and folding.
Topics: Alanine; Amino Acid Substitution; Apoproteins; Cystine; Cytochrome b Group; Cytochrome c Group; Escherichia coli; Genetic Variation; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Thermodynamics | 2000 |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.
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 |
Monitoring mobility in the early steps of unfolding: the case of oxidized cytochrome b(5) in the presence of 2 M guanidinium chloride.
Topics: Animals; Cytochromes b5; Guanidine; Heme; Kinetics; Magnetic Resonance Spectroscopy; Microsomes; Models, Molecular; Nitrogen Isotopes; Protein Conformation; Protein Denaturation; Protein Folding; Rats | 2000 |
Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties.
Topics: Amino Acid Sequence; Amino Acid Substitution; Bacteria, Aerobic; Base Sequence; Binding Sites; Cloning, Molecular; Cysteine; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Denaturation; Protein Folding; Recombinant Proteins; Templates, Genetic | 2000 |
pH dependence of formation of a partially unfolded state of a Lys 73 --> His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Titrimetry | 2000 |
Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.
Topics: Animals; Binding Sites; Cytochrome c Group; Diffusion; Dose-Response Relationship, Drug; Guanidine; Heme; Horses; Kinetics; Ligands; Methionine; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Temperature; Thermodynamics | 2001 |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique.
Topics: Animals; Bacterial Proteins; Cytochrome c Group; Guanidine; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Protein Folding | 2001 |
Dimethyl propionate ester heme-containing cytochrome b5: structure and stability.
Topics: Amino Acid Sequence; Cytochromes b5; Enzyme Stability; Guanidine; Heme; Magnetic Resonance Spectroscopy; Magnetics; Metalloporphyrins; Molecular Sequence Data; Protein Conformation; Protein Folding | 2001 |
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
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 |
The unfolding of oxidized c-type cytochromes: the instructive case of Bacillus pasteurii.
Topics: Bacillus; Cytochrome c Group; Guanidine; Heme; Hydrogen-Ion Concentration; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mitochondria; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Spectrum Analysis; Thermodynamics | 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 |
Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c.
Topics: Amino Acid Substitution; Circular Dichroism; Cytochrome c Group; Electrochemistry; Guanidine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Models, Molecular; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; Thermodynamics; Yeasts | 2003 |
[Action of various aromatic substances and nitrogen metabolites on heme synthesis in vitro].
Topics: Creatine; Creatinine; Guanidine; Guanidines; Heme; In Vitro Techniques; Indoles; Nitrogen; Phenols; Urea; Uric Acid | 1963 |
Conformational properties of the iso-1-cytochrome C denatured state: dependence on guanidine hydrochloride concentration.
Topics: Cytochromes c; Guanidine; Heme; Histidine; Isoenzymes; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2004 |
De novo design, synthesis, and function of semiartificial myoglobin conjugated with coiled-coil two-alpha-helix peptides.
Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Flavins; Guanidine; Heme; Models, Molecular; Molecular Sequence Data; Myoglobin; NAD; Peptides; Protein Conformation; Protein Denaturation; Protein Structure, Secondary; Spectrometry, Fluorescence; Structure-Activity Relationship | 2004 |
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
Topics: Amino Acid Sequence; Apoproteins; Circular Dichroism; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Thermodynamics; Tryptophan; Urea | 2005 |
The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding.
Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Paracoccus; Peroxidase; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry; Spectrophotometry, Ultraviolet; Thermodynamics | 2005 |
Reversible thermal inactivation and conformational states in denaturant guanidinium of a calcium-dependent peroxidase from Euphorbia characias.
Topics: Calcium; Enzyme Activation; Enzyme Stability; Euphorbia; Guanidine; Heme; Kinetics; Peroxidase; Plant Proteins; Protein Conformation; Protein Denaturation; Temperature | 2005 |
Dehydration in the folding of reduced cytochrome c revealed by the electron-transfer-triggered folding under high pressure.
Topics: Cytochromes c; Guanidine; Heme; Hydrophobic and Hydrophilic Interactions; Kinetics; Oxidation-Reduction; Pressure; Protein Folding; Water | 2006 |
Differential effects of alkyl- and arylguanidines on the stability and reactivity of inducible NOS heme-dioxygen complexes.
Topics: Animals; Carbon Monoxide; Enzyme Stability; Guanidine; Heme; Mice; Nitric Oxide Synthase Type II; Oxygen; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2006 |
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
Topics: Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cyanides; Guanidine; Heme; Hemoglobins; Histidine; Iron; Ligands; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Synechocystis | 2007 |
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.
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.
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.
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.
Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Heme; Histidine; Horses; Myocardium; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet | 2007 |
Reversible two-step unfolding of heme-human serum albumin: a (1)H-NMR relaxometric and circular dichroism study.
Topics: Binding Sites; Circular Dichroism; Guanidine; Heme; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Myristic Acid; Protein Conformation; Protein Denaturation; Protein Folding; Protons; Serum Albumin | 2009 |
Stability enhancement of cytochrome c through heme deprotonation and mutations.
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.
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.
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 |
Folding energy landscape of cytochrome cb562.
Topics: Biochemistry; Cytochrome b Group; Databases, Protein; Escherichia coli; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Guanidine; Heme; Kinetics; Models, Statistical; Molecular Conformation; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary | 2009 |
Guanidine hydrochloride-induced unfolding of the three heme coordination states of the CO-sensing transcription factor, CooA.
Topics: Bacterial Proteins; Biosensing Techniques; Carbon Monoxide; Circular Dichroism; DNA; Guanidine; Heme; Hemeproteins; Iron; Models, Molecular; Mutant Proteins; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Thermodynamics; Trans-Activators; Transcription Factors | 2009 |
Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes.
Topics: Animals; Carbon; Catalase; Catalytic Domain; Cattle; Electrochemistry; Electrodes; Glass; Guanidine; Heme; Hemoglobins; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Oxidation-Reduction; Peptides; Protein Denaturation; Protein Renaturation; Protein Subunits; Spectrum Analysis | 2009 |
Role of arginine guanidinium moiety in nitric-oxide synthase mechanism of oxygen activation.
Topics: Animals; Arginine; Binding Sites; Catalytic Domain; Citrulline; Enzyme Activation; Guanidine; Heme; Hydrogen Bonding; Mice; Models, Molecular; Molecular Structure; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Oxygen; Reactive Nitrogen Species; Reactive Oxygen Species; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2010 |
Ascorbate peroxidase activity of cytochrome c.
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 |
Guanidine-ferroheme coordination in the mutant protein nitrophorin 4(L130R).
Topics: Guanidine; Heme; Hemeproteins; Mutant Proteins; Organometallic Compounds; Salivary Proteins and Peptides; Water | 2012 |
Changes in the heme ligation during folding of a Geobacter sulfurreducens sensor GSU0935.
Topics: Amino Acid Substitution; Cytochrome c Group; Geobacter; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Ligands; Oxidation-Reduction; Protein Refolding; Protein Structure, Tertiary; Water | 2012 |
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions.
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 |
Thermodynamic effects of the alteration of the axial ligand on the unfolding of thermostable cytochrome C.
Topics: Catalytic Domain; Circular Dichroism; Cytochrome c Group; Electrochemical Techniques; Guanidine; Heme; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Protein Stability; Protein Unfolding; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics; Thermus thermophilus | 2013 |
Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding.
Topics: Animals; Cytochromes c; Guanidine; Heme; Horses; Hydrogen-Ion Concentration; Models, Molecular; Protein Denaturation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Temperature; Thermodynamics | 2013 |
Pre-existent asymmetry in the human cyclooxygenase-2 sequence homodimer.
Topics: Acetylation; Amino Acid Sequence; Amino Acid Substitution; Anti-Inflammatory Agents, Non-Steroidal; Arachidonic Acid; Aspirin; Celecoxib; Cyclooxygenase 2; Cyclooxygenase Inhibitors; Flurbiprofen; Guanidine; Heme; Humans; Indomethacin; Kinetics; Models, Biological; Mutant Proteins; Mutation; Naproxen; Oxygen; Palmitic Acid; Peroxidase; Protein Multimerization; Pyrazoles; Substrate Specificity; Sulfonamides | 2013 |
Low-cost equilibrium unfolding of heme proteins using 2 μl samples.
Topics: Bacterial Proteins; Binding Sites; Circular Dichroism; Cytochromes b5; Globins; Guanidine; Heme; Kinetics; Nerve Tissue Proteins; Neuroglobin; Protein Denaturation; Protein Folding; Protein Stability; Protein Unfolding; Spectrometry, Fluorescence; Structure-Activity Relationship; Thermodynamics; Truncated Hemoglobins | 2013 |
Dynamics in the heme geometry of myoglobin induced by the one-electron reduction.
Topics: Animals; Electrons; Guanidine; Heme; Horses; Metmyoglobin; Models, Molecular; Myoglobin; Oxidation-Reduction; Protein Conformation; Protein Folding; Pulse Radiolysis; Spectrum Analysis, Raman | 2014 |
Time- and NADPH-dependent inhibition of cytochrome P450 3A4 by the cyclopentapeptide cilengitide: significance of the guanidine group and accompanying spectral changes.
Topics: Adult; Cytochrome P-450 CYP3A; Enzyme Inhibitors; Female; Guanidine; Heme; Humans; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Snake Venoms | 2014 |
Structural analyses combined with small-angle X-ray scattering reveals that the retention of heme is critical for maintaining the structure of horseradish peroxidase under denaturing conditions.
Topics: Circular Dichroism; Guanidine; Heme; Horseradish Peroxidase; Models, Molecular; Protein Denaturation; Protein Structure, Tertiary; Protein Unfolding; Temperature; Urea; X-Ray Diffraction | 2017 |
Mechanism of Human Apohemoglobin Unfolding.
Topics: Apoproteins; Cloning, Molecular; Escherichia coli; Fetal Hemoglobin; Gene Expression; Glycine; Guanidine; Heme; Hemoglobin A; Hemoglobins; Humans; Kinetics; Protein Denaturation; Protein Domains; Protein Folding; Protein Multimerization; Protein Stability; Protein Structure, Secondary; Protein Unfolding; Recombinant Proteins | 2017 |
Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.
Topics: Cytochromes c; Guanidine; Heme; Kinetics; Models, Molecular; Mutagenesis; Protein Conformation, alpha-Helical; Protein Denaturation; Rhodopseudomonas | 2018 |
Crowding Milleu stabilizes apo-myoglobin against chemical-induced denaturation: Dominance of hardcore repulsions in the heme devoid protein.
Topics: Animals; Apoproteins; Dextrans; Ficoll; Guanidine; Heme; Horses; Macromolecular Substances; Myoglobin; Protein Conformation; Protein Denaturation; Protein Stability; Spectrophotometry, Ultraviolet; Thermodynamics; Urea | 2021 |