Predicting protein conformation by statistical methods

被引:14
|
作者
Simon, I
Fiser, A
Tusnády, GE
机构
[1] Hungarian Acad Sci, Inst Enzymol, BRC, H-1518 Budapest, Hungary
[2] Eotvos Lorand Univ, Dept Biol Phys, Budapest, Hungary
基金
匈牙利科学研究基金会;
关键词
amino acid sequence; statistical method; prediction; protein; structure; transmembrane protein; topology;
D O I
10.1016/S0167-4838(01)00253-9
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
The unique folded structure makes a polypeptide a functional protein. The number of known sequences is about a hundred times larger than the number of known structures and the gap is increasing rapidly. The primary goal of all structure prediction methods is to obtain structure-related information on proteins, whose structures have not been determined experimentally. Besides this goal, the development of accurate prediction methods helps to reveal principles of protein folding. Here we present a brief survey of protein structure predictions based on statistical analyses of known sequence and structure data. We discuss the background of these methods and attempt to elucidate principles, which govern structure formation of soluble and membrane proteins. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:123 / 136
页数:14
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