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NMRDyn: A Program for NMR Relaxation Studies of Protein Association

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 relax...

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Detalles Bibliográficos
Autores principales: Wang, Conan K., Schirra, Horst Joachim, Craik, David J.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583948/
https://www.ncbi.nlm.nih.gov/pubmed/19043572
http://dx.doi.org/10.1371/journal.pone.0003820
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author Wang, Conan K.
Schirra, Horst Joachim
Craik, David J.
author_facet Wang, Conan K.
Schirra, Horst Joachim
Craik, David J.
author_sort Wang, Conan K.
collection PubMed
description 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.
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spelling pubmed-25839482008-11-26 NMRDyn: A Program for NMR Relaxation Studies of Protein Association Wang, Conan K. Schirra, Horst Joachim Craik, David J. PLoS One Research Article 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. Public Library of Science 2008-11-26 /pmc/articles/PMC2583948/ /pubmed/19043572 http://dx.doi.org/10.1371/journal.pone.0003820 Text en Wang et al. http://creativecommons.org/licenses/by/4.0/ 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 properly credited.
spellingShingle Research Article
Wang, Conan K.
Schirra, Horst Joachim
Craik, David J.
NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title_full NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title_fullStr NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title_full_unstemmed NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title_short NMRDyn: A Program for NMR Relaxation Studies of Protein Association
title_sort nmrdyn: a program for nmr relaxation studies of protein association
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583948/
https://www.ncbi.nlm.nih.gov/pubmed/19043572
http://dx.doi.org/10.1371/journal.pone.0003820
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