Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics
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- 作者：Kevin W. Plaxco ; Kim T. Simons ; Ingo Ruczinski ; and David Baker
- 刊名：Biochemistry
- 出版年：2000
- 出版时间：September 19, 2000
- 年：2000
- 卷：39
- 期：37
- 页码：11177 - 11183
- 全文大小：70K
- 年卷期：v.39,no.37(September 19, 2000)
- ISSN：1520-4995
文摘
The fastest simple, single domain proteins fold a million times more rapidly than the slowest.Ultimately this broad kinetic spectrum is determined by the amino acid sequences that define these proteins,suggesting that the mechanisms that underlie folding may be almost as complex as the sequences thatencode them. Here, however, we summarize recent experimental results which suggest that (1) despite avast diversity of structures and functions, there are fundamental similarities in the folding mechanisms ofsingle domain proteins and (2) rather than being highly sensitive to the finest details of sequence, theirfolding kinetics are determined primarily by the large-scale, redundant features of sequence that determinea protein's gross structural properties. That folding kinetics can be predicted using simple, empirical,structure-based rules suggests that the fundamental physics underlying folding may be quite straightforwardand that a general and quantitative theory of protein folding rates and mechanisms (as opposed to unfoldingrates and thus protein stability) may be near on the horizon.