Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50

被引：267

作者：

Hayward, S ^{[1
]}

Lee, RA

机构：

[1] Univ E Anglia, Sch Informat Syst, Royal Soc Wolfson Bioinformat Lab, Norwich NR4 7TJ, Norfolk, England

[2] Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England

来源：

JOURNAL OF MOLECULAR GRAPHICS & MODELLING | 2002年 / 21卷 / 03期

基金：

英国工程与自然科学研究理事会;

关键词：

domain motions in proteins; proteins conformational change; DynDom; hinge bending;

D O I：

10.1016/S1093-3263(02)00140-7

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

DynDom is a program that analyses conformational change in proteins for dynamic domains, hinge axes, and hinge-bending regions. Here, a number of improvements and additions are reported which have been implemented in the new version 1.50. The most significant improvement is in the determination of the hinge-bending residues. A new routine also compares quantities relating to the main-chain dihedrals of bending residues with the hinge-bending motion. This version of the program can now be run from the DynDom website at: http://www.sys.uea.ac.uk/dyndom. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：181 / 183

页数：3

共 10 条

[1] APOLACTOFERRIN STRUCTURE DEMONSTRATES LIGAND-INDUCED CONFORMATIONAL CHANGE IN TRANSFERRINS [J].