Structural correlations in protein folding funnels

被引：117

作者：

Shoemaker, BA ^{[1
]}

Wang, J ^{[1
]}

Wolynes, PG ^{[1
]}

机构：

[1] UNIV ILLINOIS,SCH CHEM SCI,URBANA,IL 61801

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1997年 / 94卷 / 03期

关键词：

folding kinetics; transition state ensemble; extrathermodynamic free energy relations; protein structure;

D O I：

10.1073/pnas.94.3.777

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：

While the overall energy landscape of a foldable protein can be described by means of a few parameters characterizing its statistical topography, specific energetic terms subtly bias the representative structures giving rise to residue pair correlations as in a liquid. We use a free energy functional incorporating an inhomogeneous pair contact energy along with a contact formation entropy and a cooperativity contribution to determine residue-specific contact probabilities in the denatured state and the transition state ensemble. The predicted ''hot residues'' for the theoretical transition state ensemble reasonably agree with experiment for chymotrypsin inhibitor 2, and generally a strong correlation exists with the measured kinetic effects of mutating residues not involved in highly solvent-exposed regions.

引用

页码：777 / 782

页数：6

共 38 条

[1] FIRST-PRINCIPLES CALCULATION OF THE FOLDING FREE-ENERGY OF A 3-HELIX BUNDLE PROTEIN [J].