Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus
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 sol...
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| Hauptverfasser: | , , , , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
27 May 2016
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| In: |
Journal of biomolecular NMR
Year: 2016, Jahrgang: 65, Heft: 2, Pages: 87-98 |
| ISSN: | 1573-5001 |
| DOI: | 10.1007/s10858-016-0040-2 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s10858-016-0040-2
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| Verfasserangaben: | 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 |
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| 245 | 1 | 0 | |a Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus |c 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 |
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| 520 | |a 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 [2H,13C,15N]-labeled protein are shown to yield narrow 13C 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. | ||
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