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NMRDyn: a program for NMR relaxation studies of protein association
- 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.
- Subjects :
- Physics
Magnetic Resonance Spectroscopy
Multidisciplinary
Biological phenomenon
Interface (computing)
Association (object-oriented programming)
lcsh:R
Proteins
lcsh:Medicine
Nuclear magnetic resonance spectroscopy
Molecular dynamics
Biochemistry/Bioinformatics
Biochemistry/Macromolecular Assemblies and Machines
Chemical physics
Biophysics
Relaxation (physics)
Analysis software
lcsh:Q
Anisotropy
lcsh:Science
Dimerization
Biochemistry/Biomacromolecule-Ligand Interactions
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 3
- Issue :
- 11
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....4e75bed0f769c3ac9fcf2224b7ca89b9