The protein coil library: A structural database of nonhelix, nonstrand fragments derived from the PDB

被引：92

作者：

Fitzkee, NC ^{[1
]}

Fleming, PJ ^{[1
]}

Rose, GD ^{[1
]}

机构：

[1] Johns Hopkins Univ, TC Jenkins Dept Biophys, Baltimore, MD 21218 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2005年 / 58卷 / 04期

关键词：

protein structure; protein conformation; secondary structure; random coil; statistical coil;

D O I：

10.1002/prot.20394

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：

Approximately half the structure of folded proteins is either a-helix or R-strand. We have developed a convenient repository of all remaining structure after these two regular secondary structure elements are removed. The Protein Coil Library (http://roselab.jhu.edu/coil/) allows rapid and comprehensive access to non-alpha-helix and non-beta-strand fragments contained in the Protein Data Bank (PDB). The library contains both sequence and structure information together with calculated torsion angles for both the backbone and side chains. Several search options are implemented, including a query function that uses output from popular PDB-culling servers directly. Additionally, several popular searches are stored and updated for immediate access. The library is a useful tool for exploring conformational propensities, turn motifs, and a recent model of the unfolded state. (C) 2005 Wiley-Liss, Inc.

引用

页码：852 / 854

页数：3

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