Packing helices in proteins by global optimization of a potential energy function

被引：36

作者：

Nanias, M

Chinchio, M

Pillardy, J

Ripoll, DR

Scheraga, HA ^{[1
]}

机构：

[1] Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA

[2] Cornell Theory Ctr, Computat Biol Serv Unit, Ithaca, NY 14853 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 04期

关键词：

D O I：

10.1073/pnas.252760199

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：

An efficient method has been developed for packing alpha-helices in proteins. It treats alpha-helices as rigid bodies and uses a simplified Lennard-Jones potential with Miyazawa-Jernigan contact-energy parameters to describe the interactions between the alpha-helical elements in this coarse-grained system. Global conformational searches to generate packing arrangements rapidly are carried out with a Monte Carlo-with-minimization type of approach. The results for 42 proteins show that the approach reproduces native-like folds of alpha-helical proteins as low-energy local minima of this highly simplified potential function.

引用

页码：1706 / 1710

页数：5

共 22 条

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