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Comparative Study
. 2002 Dec;21(3):181-3.
doi: 10.1016/s1093-3263(02)00140-7.

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

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Comparative Study

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

Steven Hayward et al. J Mol Graph Model. 2002 Dec.

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.

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