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 journalArticle

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)
JournalAustralian Journal of Chemistry
DOIs
StateAccepted/In press - Jan 1 2019

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Nuclear magnetic resonance spectroscopy
Membrane Proteins
Lipid bilayers
G-Protein-Coupled Receptors
Linewidth
Molecular dynamics
Nuclear magnetic resonance
Topology
Peptides
Computer simulation
Proteins

Cite this

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