Ontology type: schema:ScholarlyArticle Open Access: True
2016-06
AUTHORSMarie-Laure Fogeron, Vlastimil Jirasko, Susanne Penzel, David Paul, Roland Montserret, Clément Danis, Denis Lacabanne, Aurélie Badillo, Jérôme Gouttenoire, Darius Moradpour, Ralf Bartenschlager, François Penin, Beat H. Meier, Anja Böckmann
ABSTRACTWe describe the expression of the hepatitis C virus nonstructural protein 4B (NS4B), which is an integral membrane protein, in a wheat germ cell-free system, the subsequent purification and characterization of NS4B and its insertion into proteoliposomes in amounts sufficient for multidimensional solid-state NMR spectroscopy. First spectra of the isotopically [(2)H,(13)C,(15)N]-labeled protein are shown to yield narrow (13)C resonance lines and a proper, predominantly α-helical fold. Clean residue-selective leucine, isoleucine and threonine-labeling is demonstrated. These results evidence the suitability of the wheat germ-produced integral membrane protein NS4B for solid-state NMR. Still, the proton linewidth under fast magic angle spinning is broader than expected for a perfect sample and possible causes are discussed. More... »
PAGES87-98
http://scigraph.springernature.com/pub.10.1007/s10858-016-0040-2
DOIhttp://dx.doi.org/10.1007/s10858-016-0040-2
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1046051581
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/27233794
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