Use of molecular mechanics for secondary structure prediction.: Is it possible to reveal α-helix?

被引：5

作者：

Kilosanidze, GT

Kutsenko, AS

Esipova, NG

Tumanyan, VG ^{[1
]}

机构：

[1] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow 119991, Russia

[2] Karolinska Inst, Ctr Genom & Bioinformat, S-17177 Stockholm, Sweden

来源：

FEBS LETTERS | 2002年 / 510卷 / 1-2期

基金：

俄罗斯基础研究基金会;

关键词：

protein secondary structure; structure prediction; alpha-helix; molecular mechanics;

D O I：

10.1016/S0014-5793(01)03212-4

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：

A new approach to predicting protein standard conformations is suggested. The idea consists in modeling by molecular mechanics tools a continuous alpha-helical conformation for the whole protein. The profile of energy along the model alpha-helix reveals minima corresponding to real alpha-helical segments in the Dative protein. The 3/10-helices and beta-turns including a local alpha-helical conformation may be detected as well. All alpha-helical segments in the test sample are delineated; mean residue by residue accuracy Q(3alpha) is 79%. This non-statistical approach can shed light on the physical grounds of a-helix formation. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：13 / 16

页数：4

共 15 条

[1] ICM - A NEW METHOD FOR PROTEIN MODELING AND DESIGN - APPLICATIONS TO DOCKING AND STRUCTURE PREDICTION FROM THE DISTORTED NATIVE CONFORMATION [J].