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NMRDyn: a program for NMR relaxation studies of protein association

Authors :
David J. Craik
Horst Joachim Schirra
Conan K. Wang
Source :
PLoS ONE, Vol 3, Iss 11, p e3820 (2008), PLoS ONE
Publication Year :
2008
Publisher :
Public Library of Science (PLoS), 2008.

Abstract

Self-association is an important biological phenomenon that is associated with many cellular processes. NMR relaxation measurements provide data about protein molecular dynamics at the atomic level and are sensitive to changes induced by self-association. Thus, measurements and analysis of NMR relaxation data can provide structurally resolved information on self-association that would not be accessible otherwise. Here, we present a computer program, NMRdyn, which analyses relaxation data to provide parameters defining protein self-association. Unlike existing relaxation analysis software, NMRdyn can explicitly model the monomer-oligomer equilibrium while fitting measured relaxation data. Additionally, the program is packaged with a user-friendly interface, which is important because relaxation data can often be large and complex. NMRdyn is available from http://research1t.imb.uq.edu.au/nmr/NMRdyn.

Details

Language :
English
ISSN :
19326203
Volume :
3
Issue :
11
Database :
OpenAIRE
Journal :
PLoS ONE
Accession number :
edsair.doi.dedup.....4e75bed0f769c3ac9fcf2224b7ca89b9