Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
复制标题
DOI：
10.1016/s1093-3263(02)00140-7
复制
发表时间：
2002-12-01
影响因子：
2.9
通讯作者：
Lee, RA
中科院分区：
文献类型：
--
作者：
Hayward, S;Lee, RA
DyDom是一个分析蛋白质动态结构域、铰链轴和铰链弯曲区的构象变化的程序。在这里，报告了在新版本1.50中实现的一些改进和添加。最显著的改进是在铰链弯曲残留物的测定方面。一个新的例程还比较了与弯曲残基的主链二面体有关的量和铰链弯曲运动。这个版本的程序现在可以从dyDom网站运行：http://www.sys.uea.ac.uk/dyndom.(C)2002 Elsevier Science Inc.保留所有权利。
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.