Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-06

AUTHORS

Marie-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

ABSTRACT

We 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... »

PAGES

87-98

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10858-016-0040-2

DOI

http://dx.doi.org/10.1007/s10858-016-0040-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046051581

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27233794


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