Flexibility, diversity, and cooperativity: Pillars of enzyme catalysis

Biochemistry

Volumn 50, Issue 48, 2011, Pages 10422-10430

  Hammes, Gordon G ^a   Benkovic, Stephen J ^b   Hammes Schiffer, Sharon ^b  

^a DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE AMINOTRANSFERASE; CONFORMATIONAL CHANGE; COOPERATIVITY; DIHYDROFOLATE REDUCTASE; DIVERSE PROTEINS; ENZYME CATALYSIS; ENZYME MECHANISM; ENZYME-SUBSTRATE COMPLEXES; FAST REACTION; FLUORESCENCE TECHNIQUE; FREE ENERGY SURFACE; HISTORICAL DEVELOPMENT; HYDRIDE TRANSFERS; MOLECULAR BASIS; MULTIPLE CONFORMATIONS; PROTEIN FLEXIBILITY; REACTION COORDINATES; SINGLE-MOLECULE; STEADY-STATE KINETICS; THEORETICAL INVESTIGATIONS;

CATALYSIS; CONFORMATIONS; FREE ENERGY; REACTION KINETICS;

ENZYMES;

ASPARTATE AMINOTRANSFERASE; DIHYDROFOLATE REDUCTASE; RIBONUCLEASE;

ARTICLE; ATOM; CATALYSIS; CONFORMATIONAL TRANSITION; ENERGY; ENZYME CATALYSIS; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE ANALYSIS; HUMAN; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FLEXIBILITY; PROTEIN PROCESSING; SINGLE MOLECULE FLUORESCENCE TECHNIQUE; STEADY STATE;

ASPARTATE AMINOTRANSFERASES; CATALYSIS; ENERGY METABOLISM; ESCHERICHIA COLI PROTEINS; MODELS, CHEMICAL; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 82455219011     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201486f     Document Type: Article

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