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 language | English (US) |
|---|---|
| Pages (from-to) | 246-251 |
| Number of pages | 6 |
| Journal | Australian Journal of Chemistry |
| Volume | 73 |
| Issue number | 3 |
| DOIs | |
| State | Published - 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.