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Australian Journal of Chemistry Australian Journal of Chemistry Society
An international journal for chemical science
RESEARCH ARTICLE

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

Daniel K. Weber https://orcid.org/0000-0001-8400-767X A C and Gianluigi Veglia A B
+ Author Affiliations
- Author Affiliations

A Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

B Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.

C Corresponding author. Email: dweber@umn.edu

Australian Journal of Chemistry 73(3) 246-251 https://doi.org/10.1071/CH19307
Submitted: 6 July 2019  Accepted: 17 August 2019   Published: 20 September 2019

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.


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