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Volumn 96, Issue 2-3, 2002, Pages 259-271
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Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase
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Author keywords
Association dissociation; Homomeric recombinant pyruvate decarboxylase; Kinetics; Oligomeric states; Protein folding; Thermodynamics
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Indexed keywords
DIMER;
MONOMER;
OLIGOMER;
PYRUVATE DECARBOXYLASE;
TETRAMER;
THIAMINE DERIVATIVE;
UREA;
ARTICLE;
DISSOCIATION;
ENZYME ACTIVITY;
FLOW KINETICS;
PRIORITY JOURNAL;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
THERMODYNAMICS;
YEAST;
CHEMISTRY;
CIRCULAR DICHROISM;
DIMERIZATION;
DRUG EFFECT;
ENZYMOLOGY;
KINETICS;
METABOLISM;
PROTEIN DENATURATION;
STRUCTURE ACTIVITY RELATION;
TEMPERATURE;
CIRCULAR DICHROISM;
DIMERIZATION;
KINETICS;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PYRUVATE DECARBOXYLASE;
STRUCTURE-ACTIVITY RELATIONSHIP;
TEMPERATURE;
UREA;
YEASTS;
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EID: 0037007450
PISSN: 03014622
EISSN: None
Source Type: Journal
DOI: 10.1016/S0301-4622(02)00017-0 Document Type: Article |
Times cited : (5)
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References (32)
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