Exploring the structural dynamics of proteins by pressure perturbation using macromolecular crystallography.

HPMX High pressure Macromolecular crystallography Protein dynamics Protein substates

Journal

Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271

Informations de publication

Date de publication:
2023
Historique:
medline: 27 9 2023
pubmed: 26 9 2023
entrez: 25 9 2023
Statut: ppublish

Résumé

High pressure is a convenient thermodynamic parameter to probe the dynamics of proteins as it is intimately related to volume which is essential for protein function. To be biologically active, a protein fluctuates between different substates. Pressure perturbation can promote some hidden substates by modifying the population between them. High pressure macromolecular crystallography (HPMX) is a perfect tool to capture and to characterize such substates at a molecular level providing new insights on protein dynamics. The present chapter describes the use of the diamond anvil cell to perform HPMX experiments. It also provides tips on sample preparation and optimal data collection as well as on efficient analysis of the resulting high-pressure structures.

Identifiants

pubmed: 37748831
pii: S0076-6879(23)00212-4
doi: 10.1016/bs.mie.2023.06.007
pii:
doi:

Substances chimiques

Macromolecular Substances 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

349-381

Informations de copyright

Copyright © 2023. Published by Elsevier Inc.

Auteurs

Nathalie Colloc'h (N)

Imagerie et stratégies thérapeutiques pour les cancers et tissus cérébraux (ISTCT), CNRS Université de Caen Normandie, Centre Cyceron, Caen, France.

Anne-Claire Dhaussy (AC)

Normandie Université, CRISMAT UMR, Caen, France.

Eric Girard (E)

Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France. Electronic address: eric.girard@ibs.fr.

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Classifications MeSH