NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.
Allostery
Chemical exchange
Nuclear magnetic resonance (NMR) spectroscopy
Phosphopeptides
Protein dynamics
Spin relaxation
Src-homology 2 (SH2) domain
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
medline:
6
9
2023
pubmed:
5
9
2023
entrez:
5
9
2023
Statut:
ppublish
Résumé
Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond-millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R
Identifiants
pubmed: 37668967
doi: 10.1007/978-1-0716-3393-9_2
doi:
Substances chimiques
Phosphopeptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
25-37Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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