Cytochrome c553, a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics

Journal of Molecular Biology

Volumn 301, Issue 4, 2000, Pages 769-773

  Guidry, Jesse ^a   Wittung Stafshede, Pernilla ^a  

^a Tulane University   (United States)

Author keywords

Cytochrome; Heme; Kinetics; Protein folding; Stopped flow

Indexed keywords

CYTOCHROME; HEMOPROTEIN; HISTIDINE; METHIONINE; CYTOCHROME C; CYTOCHROME C553; GUANIDINE; WATER;

ARTICLE; CHEMICAL REACTION KINETICS; CONFORMATIONAL TRANSITION; DESULFOVIBRIO VULGARIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; KINETICS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN DENATURATION; PROTEIN RENATURATION; THERMODYNAMICS;

DESULFOVIBRIO VULGARIS;

CYTOCHROME C GROUP; DESULFOVIBRIO VULGARIS; GUANIDINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; METHIONINE; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; THERMODYNAMICS; WATER;

EID: 0034713930     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3993     Document Type: Article

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