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Flexibility, diversity, and cooperativity: Pillars of enzyme catalysis
Gordon G. Hammes
,
Stephen J. Benkovic
, Sharon Hammes-Schiffer
Chemistry
Research output
:
Contribution to journal
›
Article
›
peer-review
245
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Scopus citations
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Keyphrases
Cooperativity
100%
Enzyme Catalysis
100%
Conformational Change
66%
Methylenetetrahydrofolate Reductase (MTHFR)
66%
Fast Reactions
33%
Ribonuclease
33%
General Mechanism
33%
Fluorescence Method
33%
Aspartate Aminotransferase
33%
Nuclear Magnetic Resonance
33%
Historical Development
33%
Steady-state Kinetics
33%
Hydride Transfer
33%
Standard Free Energy
33%
Protein Flexibility
33%
Single-molecule Fluorescence
33%
Reaction Coordinate
33%
Enzyme-substrate Complex
33%
Protein Conformation
33%
Free Energy Surface
33%
Enzyme Mechanism
33%
Multiple Conformations
33%
Biochemistry, Genetics and Molecular Biology
Cooperation
100%
Enzyme Catalysis
100%
Conformational Change
66%
Dihydrofolate Reductase
66%
Conformation
33%
Steady State
33%
Ribonuclease
33%
Aspartate Transaminase
33%
Enzyme Mechanism
33%
Protein Conformation
33%
Enzyme Substrate Complex
33%
Magnetism
33%
Chemistry
Dihydrofolates
100%
NMR Spectroscopy
50%
Aspartate
50%
Protein Conformation
50%
Aspartic Acid
50%
Surface Free Energy
50%
Material Science
Catalysis
100%
Nuclear Magnetic Resonance
33%
Surface Energy
33%
Hydride
33%
Protein Conformation
33%