Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding

被引：378

作者：

Hagen, SJ ^{[1
]}

Hofrichter, J ^{[1
]}

Szabo, A ^{[1
]}

Eaton, WA ^{[1
]}

机构：

[1] NIDDKD,PHYS CHEM LAB,NIH,BETHESDA,MD 20892

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 21期

关键词：

laser photolysis; polymer dynamics;

D O I：

10.1073/pnas.93.21.11615

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

How fast can a protein fold? The rate of polypeptide collapse to a compact state sets an upper limit to the rate of folding. Collapse may in turn be limited by the rate of intrachain diffusion. To address this question, we have determined the rate at which two regions of an unfolded protein are brought into contact by diffusion. Our nanosecond-resolved spectroscopy shows that under strongly denaturing conditions, regions of unfolded cytochrome c separated by similar to 50 residues diffuse together in 35-40 mu s. This result leads to an estimate of similar to (1 mu s)(-1) as the upper limit for the rate of protein folding.

引用

页码：11615 / 11617

页数：3

共 43 条

[1] KINETIC-ANALYSIS OF FOLDING AND UNFOLDING THE 56-AMINO ACID IGG-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN-G [J].