title: Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50.
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.
authors.affiliation: Royal Society-Wolfson Bioinformatics Laboratory, School of Information Systems, University of East Anglia, Norwich NR4 7TJ, UK. sjh@sys.uea.ac.uk
authors.forename: Steven
authors.initials: S
authors.lastname: Hayward
authors.forename: Richard A
authors.initials: RA
authors.lastname: Lee
mesh_terms: 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
chemical_list: D007143:Immunoglobulin Heavy Chains