title: NMRDyn: a program for NMR relaxation studies of protein association.
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.
authors.affiliation: The University of Queensland, Institute for Molecular Bioscience, Brisbane, Queensland, Australia.
authors.forename: Conan K
authors.initials: CK
authors.lastname: Wang
authors.forename: Horst Joachim
authors.initials: HJ
authors.lastname: Schirra
authors.forename: David J
authors.initials: DJ
authors.lastname: Craik
mesh_terms: D019281:Dimerization; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011506:Proteins