Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50.
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.
Hayward
Steven
S
Royal Society-Wolfson Bioinformatics Laboratory, School of Information Systems, University of East Anglia, Norwich NR4 7TJ, UK. sjh@sys.uea.ac.uk
Lee
Richard A
RA
D000465:Algorithms; D000818:Animals; D016000:Cluster Analysis; D018360:Crystallography, X-Ray; D004285:Dogs; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry*; D008223:Lymphoma / Q000737:chemistry; D008958:Models, Molecular; D009038:Motion; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D007143:Immunoglobulin Heavy Chains