Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Biochim Biophys Acta
; 1838(3): 784-92, 2014 Mar.
Article
en En
| MEDLINE
| ID: mdl-24192053
Palabras clave
1,4-dithio-D-threitol; 1-palmitoyl-2-hydroxy-sn-glycero-3-phospho-(1'-rac-glycerol); 4,4-dimethyl-4-silapentane-1-sulfonic acid; CD; CPMG; CarrPurcellMeiboomGil (pulse-train); DHPC; DPC; DSS; DTT; Envelope glycoproteins; HCV; HSQC; Hepatitis C virus; IPTG; LPPG; MBP; MP; Membrane-associated proteins; NMR; Nuclear magnetic resonance; Protein structure; SDS; TEV; TM; Transmembrane helix; circular dichroism; dihexanoylphosphatidylcholine; dodecyl-phosphocholine; hepatitis C virus; heteronuclear single-quantum coherence; isopropyl ß-D-1-thiogalactopyranoside; maltose-binding protein; membrane-embedded protein; nuclear magnetic resonance; sodium dodecylsulphate; tobacco etch virus (protease); transmembrane domain
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Membrana Celular
/
Proteínas del Envoltorio Viral
/
Resonancia Magnética Nuclear Biomolecular
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
2014
Tipo del documento:
Article
País de afiliación:
Israel