15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale.
Journal
Journal of visualized experiments : JoVE
ISSN: 1940-087X
Titre abrégé: J Vis Exp
Pays: United States
ID NLM: 101313252
Informations de publication
Date de publication:
19 04 2021
19 04 2021
Historique:
entrez:
3
5
2021
pubmed:
4
5
2021
medline:
17
6
2021
Statut:
epublish
Résumé
Protein conformational dynamics play fundamental roles in regulation of enzymatic catalysis, ligand binding, allostery, and signaling, which are important biological processes. Understanding how the balance between structure and dynamics governs biological function is a new frontier in modern structural biology and has ignited several technical and methodological developments. Among these, CPMG relaxation dispersion solution NMR methods provide unique, atomic-resolution information on the structure, kinetics, and thermodynamics of protein conformational equilibria occurring on the µs-ms timescale. Here, the study presents detailed protocols for acquisition and analysis of a
Identifiants
pubmed: 33938889
doi: 10.3791/62395
pmc: PMC8168574
mid: NIHMS1700314
doi:
Substances chimiques
Nitrogen Isotopes
0
Nitrogen-15
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM133488
Pays : United States
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