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

J Mol Graph Model. 2002 Dec;21(3):181-3. doi: 10.1016/s1093-3263(02)00140-7.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Animals
  • Cluster Analysis
  • Crystallography, X-Ray
  • Dogs
  • Immunoglobulin Heavy Chains / chemistry*
  • Lymphoma / chemistry
  • Models, Molecular
  • Motion*
  • Protein Binding
  • Protein Conformation*
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Structure-Activity Relationship

Substances

  • Immunoglobulin Heavy Chains