Fast kinetics and mechanisms in protein folding

被引：435

作者：

Eaton, WA ^{[1
]}

Muñoz, V ^{[1
]}

Hagen, SJ ^{[1
]}

Jas, GS ^{[1
]}

Lapidus, LJ ^{[1
]}

Henry, ER ^{[1
]}

Hofrichter, J ^{[1
]}

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2000年 / 29卷

关键词：

laser-triggering; temperature-jump; fast mixing; secondary structure; kinetic models;

D O I：

10.1146/annurev.biophys.29.1.327

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This review describes how kinetic experiments using techniques with dramatically improved time resolution have contributed to understanding mechanisms in protein folding. Optical triggering with nanosecond laser pulses has made it possible to study the fastest-folding proteins as well as fundamental processes in folding for the first time. These include formation of alpha-helices, beta-sheets, and contacts between residues distant in sequence, as well as overall collapse of the polypeptide chain. Improvements in the time resolution of mixing experiments and the use of dynamic nuclear magnetic resonance methods have also allowed kinetic studies of proteins that fold too fast (greater than or similar to 10(3) s(-1)) to be observed by conventional methods. Simple statistical mechanical models have been extremely useful in interpreting the experimental results. One of the surprises is that models originally developed for explaining the fast kinetics of secondary structure formation in isolated peptides are also successful in calculating folding rates of single domain proteins from their native three-dimensional structure.

引用

页码：327 / 359

页数：33

共 132 条

[1] Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures [J].