nmrdyn a program for nmr relaxation studies of protein associationnmrdyn蛋白质的核磁共振弛豫研究项目协会.pdfVIP

NMRDyn: A Program for NMR Relaxation Studies of Protein Association Conan K. Wang, Horst Joachim Schirra, David J. Craik* The University of Queensland, Institute for Molecular Bioscience, Brisbane, Queensland, Australia 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 .au/nmr/NMRdyn. Citation: Wang CK, Schirra HJ, Craik DJ (2008) NMRDyn: A Program for NMR Relaxation Studies of Protein Association. PLoS ONE 3(11): e3820. doi:10.1371/ journal.pone.0003820 Editor: Bostjan Kobe, University of Queensland, Australia Received June 30, 2008; Accepted November 7, 2008; Published November 26, 2008 Copyright: 2008 Wang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: Australian Research Council. The funders had no role in study design, data collection and analysis, decision to publish, or p