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Updated: Sep 28, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
Steven Hayward1, Richard A Lee
1Royal Society-Wolfson Bioinformatics Laboratory, School of Information Systems, University of East Anglia, Norwich NR4 7TJ, UK. sjh@sys.uea.ac.uk
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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