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Updated: Jul 19, 2026

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
Published on: July 16, 2012
Spectroscopic study of conformational changes accompanying self-assembly of HCV core protein
Arantxa Rodríguez-Casado1, Marina Molina, Pedro Carmona
1Instituto de Estructura de la Materia (CSIC), Serrano 121, 28006 Madrid, Spain.
Abstract:
Electron microscopy and infrared and Raman spectroscopy have been used here to study the morphology, size distribution, secondary and tertiary structures of protein particles assembled from a truncated hepatitis C virus (HCV) core protein covering the first 120 aa. Particles of pure protein, having similar morphology and size distribution of those of nucleocapsids found in sera from HCV-infected patients, have been visualized for the first time. The secondary structure of these protein particles involve beta-sheet enrichment in relation to its protein monomer. Tertiary/quaternary structure has also been studied using the dynamics of H/D exchange. With this aim infrared spectra were measured as a function of H/D exchange time and subsequently analyzed by principal component analysis and two-dimensional correlation spectroscopy. Temporal dynamics of exchange for these protein particles were as follows: arginine residues exchanged first, followed by turn and unordered structures, followed by beta-sheets which may act as linkers of protein monomers.
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