scholarly journals Direct Determination of a Molecular Torsional Angle in the Membrane Protein Rhodopsin by Solid-State NMR

1997 ◽  
Vol 119 (29) ◽  
pp. 6853-6857 ◽  
Author(s):  
X. Feng ◽  
P. J. E. Verdegem ◽  
Y. K. Lee ◽  
D. Sandström ◽  
M. Edén ◽  
...  
1996 ◽  
Vol 257 (3-4) ◽  
pp. 314-320 ◽  
Author(s):  
X. Feng ◽  
Y.K. Lee ◽  
D. Sandstrom ◽  
M. Edén ◽  
H. Maisel ◽  
...  

1997 ◽  
Vol 119 (49) ◽  
pp. 12006-12007 ◽  
Author(s):  
X. Feng ◽  
M. Edén ◽  
A. Brinkmann ◽  
H. Luthman ◽  
L. Eriksson ◽  
...  

2013 ◽  
Vol 10 (10) ◽  
pp. 1007-1012 ◽  
Author(s):  
Shenlin Wang ◽  
Rachel A Munro ◽  
Lichi Shi ◽  
Izuru Kawamura ◽  
Takashi Okitsu ◽  
...  

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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