Prediction of protein secondary structure content

被引:102
作者
Liu, WM [1 ]
Chou, KC
机构
[1] Pharmacia & Upjohn Inc, Comp Aided Drug Discovery, Kalamazoo, MI 49007 USA
[2] Indiana Univ Purdue Univ, Dept Comp & Informat Sci, Indianapolis, IN 46202 USA
来源
PROTEIN ENGINEERING | 1999年 / 12卷 / 12期
关键词
1st-order coupled components; alpha-helix; beta-sheet; beta-bridge; 3(10)-helix; pi-helix; H-bonded turn; bend; random coil;
D O I
10.1093/protein/12.12.1041
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
All existing algorithms for predicting the content of protein secondary structure elements have been based on the conventional amino-acid-composition, where no sequence coupling effects are taken into account. In this article,,an algorithm was developed for predicting the content of protein secondary structure elements that was based on a new amino-acid-composition, in which the sequence coupling effects are explicitly included through a series of conditional probability elements. The prediction was examined:by a self-consistency test and an independent dataset test. Both indicated a remarkable improvement obtained when using the current algorithm to predict the contents of alpha-helix, beta-sheet, beta-bridge, 3(10)-helix, pi-helix, H-bonded turn,bend and random coil. Examples of the improved accuracy by introducing the new amino-acid-composition, as well as,its impact on the study of protein structural class and biologically function, are discussed.
引用
收藏
页码:1041 / 1050
页数:10
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