简单单结构域蛋白质的折叠速率常数如何取决于天然接触的数量。
How the folding rate constant of simple, single-domain proteins depends on the number of native contacts.
作者信息
Makarov Dmitrii E, Keller Craig A, Plaxco Kevin W, Metiu Horia
机构信息
Department of Chemistry and Biochemistry, University of Texas, Austin, TX 78712, USA.
出版信息
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3535-9. doi: 10.1073/pnas.052713599.
Abstract
Experiments have shown that the folding rate constants of two dozen structurally unrelated, small, single-domain proteins can be expressed in terms of one quantity (the contact order) that depends exclusively on the topology of the folded state. Such dependence is unique in chemical kinetics. Here we investigate its physical origin and derive the approximate formula ln(k) = ln(N) + a + bN, were N is the number of contacts in the folded state, and a and b are constants whose physical meaning is understood. This formula fits well the experimentally determined folding rate constants of the 24 proteins, with single values for a and b.
摘要
实验表明，二十多种结构不相关的小单域蛋白质的折叠速率常数可以用一个仅取决于折叠态拓扑结构的量（接触序）来表示。这种依赖性在化学动力学中是独一无二的。在此，我们研究其物理起源，并推导出近似公式ln(k) = ln(N) + a + bN，其中N是折叠态中的接触数，a和b是具有明确物理意义的常数。该公式能很好地拟合这24种蛋白质实验测定的折叠速率常数，a和b为单一值。
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