期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 100, 期 22, 页码 12678-12682出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1735417100
关键词
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资金
- NIGMS NIH HHS [GM 34993, R01 GM034993] Funding Source: Medline
Proteins are complex molecules, yet their folding kinetics is often fast (microseconds) and simple, involving only a single exponential function of time (called two-state kinetics). The main model for two-state kinetics has been transition-state theory, where an energy barrier defines a slow step to reach an improbable structure. But how can barriers explain fast processes, such as folding? We study a simple model with rigorous kinetics that explains the high speed instead as a result of the microscopic parallelization of folding trajectories. The single exponential results from a separation of timescales; the parallelization of routes is high at the start of folding and low thereafter. The ensemble of rate-limiting chain conformations is different from in transition-state theory; it is broad, overlaps with the denatured state, is not aligned along a single reaction coordinate, and involves well populated, rather than improbable, structures.
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