Nonexponential structural relaxations in proteins

被引：67

作者：

Hagen, SJ

Eaton, WA

机构：

[1] Laboratory of Chemical Physics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda

来源：

JOURNAL OF CHEMICAL PHYSICS | 1996年 / 104卷 / 09期

关键词：

D O I：

10.1063/1.471044

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Conformational changes in proteins have been observed to exhibit a nonexponential time course. In myoglobin the conformational relaxation that follows photodissociation of the heme ligand is a very extended process that stretches from less than 1 picosecond to nearly 1 microsecond. We explain these kinetics with a model in which the initial protein conformational substates are connected to the final substates and to each other via transition states of a single energy. (C) 1996 American Institute of Physics.

引用

页码：3395 / 3398

页数：4

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