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A Theoretical Assessment of the Structure Determination of Multi-Span Membrane Proteins by Oriented Sample Solid-State NMR Spectroscopy
Author(s) -
Daniel K. Weber,
Gianluigi Veglia
Publication year - 2020
Publication title -
australian journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.319
H-Index - 77
eISSN - 1445-0038
pISSN - 0004-9425
DOI - 10.1071/ch19307
Subject(s) - chemistry , membrane protein , spectroscopy , solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , membrane , chemical physics , analytical chemistry (journal) , crystallography , nuclear magnetic resonance , chromatography , stereochemistry , physics , biochemistry , quantum mechanics
Oriented sample solid state NMR (OS-ssNMR) spectroscopy allows direct determination of the structure and topology of membrane proteins reconstituted into aligned lipid bilayers. While OS-ssNMR theoretically has no upper size limit, its application to multi-span membrane proteins has not been established since 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 [ 15 N- 1 H] 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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