Quantifying Microsecond Exchange in Large Protein Complexes with Accelerated Relaxation Dispersion Experiments in the Solid State.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
31 07 2019
Historique:
received: 15 01 2019
accepted: 16 07 2019
entrez: 2 8 2019
pubmed: 2 8 2019
medline: 21 10 2020
Statut: epublish

Résumé

Solid state NMR is a powerful method to obtain information on the structure and dynamics of protein complexes that, due to solubility and size limitations, cannot be achieved by other methods. Here, we present an approach that allows the quantification of microsecond conformational exchange in large protein complexes by using a paramagnetic agent to accelerate

Identifiants

pubmed: 31366983
doi: 10.1038/s41598-019-47507-8
pii: 10.1038/s41598-019-47507-8
pmc: PMC6668460
doi:

Substances chimiques

Immunoglobulin G 0
Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

11082

Subventions

Organisme : NIGMS NIH HHS
ID : P41 GM103311
Pays : United States
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L022761/1
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R01 GM129325
Pays : United States
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R010218/1
Pays : United Kingdom

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Auteurs

Carl Öster (C)

Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.

Simone Kosol (S)

Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.

Józef R Lewandowski (JR)

Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK. j.r.lewandowski@warwick.ac.uk.

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