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Spectroscopic study of conformational changes accompanying self‐assembly of HCV core protein
Author(s) -
RodríguezCasado Arantxa,
Molina Marina,
Carmona Pedro
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21192
Subject(s) - core (optical fiber) , chemistry , core protein , biophysics , crystallography , virology , computational biology , materials science , biochemistry , biology , composite material
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 β‐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 β‐sheets which may act as linkers of protein monomers. Proteins 2007. © 2006 Wiley‐Liss, Inc.