期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 14, 期 5, 页码 644-651出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2010.07.020
关键词
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资金
- NIH [GM56207, 1R01GM092946]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM056207, R37GM056207, R01GM092946] Funding Source: NIH RePORTER
Recently, the hypothesis that protein motions are involved in enzymatic turnover has gained significant attention. We review cases where there is evidence that protein motions are rate-limiting in the overall catalytic cycle and examine experimental and theoretical evidence for how such motions enhance the probability of sampling the transition state configurations relative to the ground state. The impact of tunneling, the possible role of vibrational coupling and the value of conformational chemical landscapes are also scrutinized.
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