Combined SANS & NMR studies of seven transmembrane helical proteins in native-like membrane mimetic environment using isotope labelling
Structure determination of membrane proteins is challenging, accounting for <1% of the unique protein structures deposited in the PDB. In addition, most of these structures were not obtained in a native-like environment, adding doubt to their physiological relevance. Recently, a novel membrane mimetic, the lipodisq, has been developed that could enable the study of integral membrane proteins in a native-like bilayer environment by both NMR and SANS methods. We propose to insert a seven transmembrane helical receptor, bacteriorhodopsin, into lipodisqs and acquire high-resolution solution NMR spectra and low resolution SANS measurements of bacteriorhodopsin while in a 'stealth' carrier. If this is successful it will pave the way for many more structures of membrane proteins in native-like environments to be solved. Here we request beamtime to conduct SANS contrast variation experiments at ILL on the lipodisq-protein complex, which could provide novel and complementary data on the structure and oligomeric state of bacteriorhodopsin while in the novel lipodisqs.
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WATTS Anthony; BADA Juan Francisco; Juliette M. Devos; FORSYTH Victor Trevor; HAERTLEIN Michael and SCHWEINS Ralf. (2015). Combined SANS & NMR studies of seven transmembrane helical proteins in native-like membrane mimetic environment using isotope labelling. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-732
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