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

Hayward, Steven ORCID: https://orcid.org/0000-0001-6959-2604 and Lee, Richard A. (2002) Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. Journal of Molecular Graphics and Modelling, 21 (3). pp. 181-183. ISSN 1093-3263

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Abstract

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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Computing Sciences
Faculty of Science > School of Biological Sciences
Depositing User: Vishal Gautam
Date Deposited: 28 Feb 2011 10:51
Last Modified: 26 Sep 2022 03:39
URI: https://ueaeprints.uea.ac.uk/id/eprint/21738
DOI: 10.1016/S1093-3263(02)00140-7

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