期刊
SCIENCE
卷 301, 期 5637, 页码 1196-1202出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1085515
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资金
- NIGMS NIH HHS [GM56207, GM24129, GM13306] Funding Source: Medline
The seminal hypotheses proposed over the years for enzymatic catalysis are scrutinized. The historical record is explored from both biochemical and theoretical perspectives. Particular attention is given to the impact of molecular motions within the protein on the enzyme's catalytic properties. A case study for the enzyme dihydrofolate reductase provides evidence for coupled networks of predominantly conserved residues that influence the protein structure and motion. Such coupled networks have important implications for the origin and evolution of enzymes, as well as for protein engineering.
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