Localizing frustration in native proteins and protein assemblies

被引：265

作者：

Ferreiro, Diego U. ^{[1
,2
]}

Hegler, Joseph A. ^{[1
,2
]}

Komives, Elizabeth A. ^{[2
]}

Wolynes, Peter G. ^{[1
,2
]}

机构：

[1] Univ Calif San Diego, Ctr Theoret Biol Phys, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 50期

关键词：

protein folding; protein function; energy landscape;

D O I：

10.1073/pnas.0709915104

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：

We propose a method of quantifying the degree of frustration manifested by spatially local interactions in protein biomolecules. This method of localization smoothly generalizes the global criterion for an energy landscape to be funneled to the native state, which is in keeping with the principle of minimal frustration. A survey of the structural database shows that natural proteins are multiply connected by a web of local interactions that are individually minimally frustrated. In contrast, highly frustrated interactions are found clustered on the surface, often near binding sites. These binding sites become less frustrated upon complex formation.

引用

页码：19819 / 19824

页数：6

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