DNP NMR of biomolecular assemblies.
Biological assemblies
Dynamic nuclear polarization
Magic angle spinning
Protein structure and dynamics
Solid-state NMR
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
01 04 2019
01 04 2019
Historique:
received:
29
06
2018
revised:
13
09
2018
accepted:
27
09
2018
pubmed:
3
10
2018
medline:
2
6
2020
entrez:
2
10
2018
Statut:
ppublish
Résumé
Dynamic Nuclear Polarization (DNP) is an effective approach to alleviate the inherently low sensitivity of solid-state NMR (ssNMR) under magic angle spinning (MAS) towards large-sized multi-domain complexes and assemblies. DNP relies on a polarization transfer at cryogenic temperatures from unpaired electrons to adjacent nuclei upon continuous microwave irradiation. This is usually made possible via the addition in the sample of a polarizing agent. The first pioneering experiments on biomolecular assemblies were reported in the early 2000s on bacteriophages and membrane proteins. Since then, DNP has experienced tremendous advances, with the development of extremely efficient polarizing agents or with the introduction of new microwaves sources, suitable for NMR experiments at very high magnetic fields (currently up to 900 MHz). After a brief introduction, several experimental aspects of DNP enhanced NMR spectroscopy applied to biomolecular assemblies are discussed. Recent demonstration experiments of the method on viral capsids, the type III and IV bacterial secretion systems, ribosome and membrane proteins are then described.
Identifiants
pubmed: 30273657
pii: S1047-8477(18)30271-5
doi: 10.1016/j.jsb.2018.09.011
pii:
doi:
Substances chimiques
Capsid Proteins
0
Free Radicals
0
Membrane Proteins
0
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
90-98Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.