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

Steven Hayward; Richard A. Lee

doi:10.1016/S1093-3263(02)00140-7

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

Steven Hayward
, Richard A. Lee

Research output: Contribution to journal › Article › peer-review

265 Citations (Scopus)

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.

Original language	English
Pages (from-to)	181-183
Number of pages	3
Journal	Journal of Molecular Graphics and Modelling
Volume	21
Issue number	3
DOIs	https://doi.org/10.1016/S1093-3263(02)00140-7
Publication status	Published - Dec 2002

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10.1016/S1093-3263(02)00140-7

Cite this

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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.",

author = "Steven Hayward and Lee, \{Richard A.\}",

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AB - 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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DO - 10.1016/S1093-3263(02)00140-7

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