A Theoretical Assessment of the Structure Determination of Multi-Span Membrane Proteins by Oriented Sample Solid-State NMR Spectroscopy

Daniel K. Weber, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Oriented sample solid-state NMR (OS-ssNMR) spectroscopy allows the direct determination of the structure and topology of membrane proteins reconstituted into aligned lipid bilayers. Although OS-ssNMR theoretically has no upper size limit, its application to multi-span membrane proteins has not been established because most studies have been restricted to single- or dual-span proteins and peptides. Here, we present a critical assessment of the application of this method to multi-span membrane proteins. We used molecular dynamics simulations to back-calculate [15N-1H] separated local field (SLF) spectra from a G protein-coupled receptor (GPCR) and show that fully resolved spectra can be obtained theoretically for a multi-span membrane protein with currently achievable resonance linewidths.

Original languageEnglish (US)
Pages (from-to)246-251
Number of pages6
JournalAustralian Journal of Chemistry
Volume73
Issue number3
DOIs
StatePublished - Mar 2020

Bibliographical note

Funding Information:
This work was partially supported by the National Institutes of Health (GM64742 and HL144130 to G. V.) and the American Heart Association (19POST34420009 to D.K.W.).

Publisher Copyright:
© 2020 CSIRO.

Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.

PubMed: MeSH publication types

  • Journal Article

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