Oriented-Sample NMR of Membrane Proteins: Sensitivity Enhancement and Spectroscopic Assignment

Author(s):  
Alexander A. Nevzorov
2010 ◽  
Vol 114 (15) ◽  
pp. 5089-5095 ◽  
Author(s):  
T. Gopinath ◽  
Raffaello Verardi ◽  
Nathaniel J. Traaseth ◽  
Gianluigi Veglia

2021 ◽  
Vol 111 ◽  
pp. 101701
Author(s):  
Joel Lapin ◽  
Emmanuel O. Awosanya ◽  
Richard J.A. Esteves ◽  
Alexander A. Nevzorov

2020 ◽  
Vol 73 (3) ◽  
pp. 246 ◽  
Author(s):  
Daniel K. Weber ◽  
Gianluigi Veglia

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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