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Solid state NMR of membrane proteins: Methods and applications

Yeh, Vivien; Bonev, Boyan B.

Solid state NMR of membrane proteins: Methods and applications Thumbnail


Authors

Vivien Yeh



Abstract

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

Citation

Yeh, V., & Bonev, B. B. (2021). Solid state NMR of membrane proteins: Methods and applications. Biochemical Society Transactions, 49(4), 1505-1513. https://doi.org/10.1042/BST20200070

Journal Article Type Article
Acceptance Date Jul 27, 2021
Online Publication Date Aug 16, 2021
Publication Date Aug 1, 2021
Deposit Date Aug 17, 2021
Publicly Available Date Aug 2, 2022
Journal Biochemical Society Transactions
Print ISSN 0300-5127
Electronic ISSN 1470-8752
Publisher Portland Press
Peer Reviewed Peer Reviewed
Volume 49
Issue 4
Pages 1505-1513
DOI https://doi.org/10.1042/BST20200070
Keywords Biochemistry
Public URL https://nottingham-repository.worktribe.com/output/6055663
Publisher URL https://portlandpress.com/biochemsoctrans/article-abstract/doi/10.1042/BST20200070/229562/Solid-state-NMR-of-membrane-proteins-methods-and?redirectedFrom=fulltext
Additional Information This is not the final peer-reviewed version of record.

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