Conformational features of truncated hepatitis C virus core protein in virus-like particles.
HCVc 120 is a truncated protein from the hepatitis C virus (HCV) core protein that interacts with itself to form nucleocapsid-like particles. We present here the infrared and Raman spectra of oligomeric HCVc 120 protein in order to obtain insights into its secondary structure as well as the environment surrounding some protein side chains. When compared with its monomer form, oligomeric HCVc 120 protein shows an increase in beta-sheet structure. Tryptophan residues have been found to be solvent exposed in the oligomeric form, and they likely do not significantly participate in the protein assembly. However, the beta-sheet content in oligomeric HCVc 120 protein suggests that this structural motif cannot be excluded in nucleocapsid formation, as shown recently in other viruses.
Instituto de Estructura de la Materia (CSIC), Serrano 121, 28006 Madrid, Spain.
A
A
Rodriguez-Casado
Marina
M
Molina
Pedro
P
Carmona
D019281:Dimerization; D016174:Hepacivirus / Q000737:chemistry* / Q000378:metabolism; D019251:Nucleocapsid / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared / Q000379:methods; D013059:Spectrum Analysis, Raman / Q000379:methods; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism; D014771:Virion / Q000737:chemistry / Q000378:metabolism; D019065:Virus Assembly
D014758:Viral Core Proteins; C069130:nucleocapsid protein, Hepatitis C virus