Protein resonance assignment by BSH-CP-based 3D solid-state NMR experiments: A practical guide.
BSH-CP
magic-angle spinning
protein NMR
resonance assignment
solid-state NMR
Journal
Magnetic resonance in chemistry : MRC
ISSN: 1097-458X
Titre abrégé: Magn Reson Chem
Pays: England
ID NLM: 9882600
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
14
01
2019
revised:
05
07
2019
accepted:
17
09
2019
pubmed:
7
11
2019
medline:
11
11
2020
entrez:
7
11
2019
Statut:
ppublish
Résumé
Solid-state NMR (ssNMR) spectroscopy has evolved into a powerful method to obtain structural information and to study the dynamics of proteins at atomic resolution and under physiological conditions. The method is especially well suited to investigate insoluble and noncrystalline proteins that cannot be investigated easily by X-ray crystallography or solution NMR. To allow for detailed analysis of ssNMR data, the assignment of resonances to the protein atoms is essential. For this purpose, a set of three-dimensional (3D) spectra needs to be acquired. Band-selective homo-nuclear cross-polarization (BSH-CP) is an effective method for magnetization transfer between carbonyl carbon (CO) and alpha carbon (CA) atoms, which is an important transfer step in multidimensional ssNMR experiments. This tutorial describes the detailed procedure for the chemical shift assignment of the backbone atoms of
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
445-465Subventions
Organisme : European Research Council
Pays : International
Organisme : Max Planck Society
Pays : International
Organisme : Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Pays : International
Informations de copyright
© 2019 The Authors. Magnetic Resonance in Chemistry published by John Wiley & Sons Ltd.
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