Thread: NMR paper A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.
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Default A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.
A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.

Related Articles A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.

Aust J Chem. 2020;73(3):246-251

Authors: Weber DK, Veglia G

Abstract
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 [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.


PMID: 33162560 [PubMed]



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