Solid-state NMR and Membrane Proteins
Solid-state NMR and Membrane Proteins
Publication date: Available online 29 December 2014 Source:Journal of Magnetic Resonance</br> Author(s): Stanley J. Opella</br> The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects solid-state NMR, and the chemical shift and homo- and hetero- nuclear dipole-dipole interactions. Solid-state NMR has advanced sufficiently to enable the structures of membrane proteins to be determined under near-native conditions in phospholipid bilayers. Graphical abstract http://origin-ars.els-cdn.com/conten...00336X-fx1.jpg</br></br> </br></br> More... |
All times are GMT. The time now is 01:56 PM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013