Structure and dynamics changes induced by 2,2,2-trifluoro-ethanol (TFE) on the N-terminal half of hepatitis C virus core protein.
The Core protein of hepatitis C virus is involved in several interactions other than the encapsidation of viral RNA. We recently proposed that this is related to the fact that the N-terminal half of this protein (C82) is an intrinsically unstructured protein (IUP) domain. IUP domains can adopt a secondary structure when they are interacting with another molecule, such as a nucleic acid or a protein. It is also possible to mimic these conditions by modifying the environment of the protein. We investigated the propensity of this protein to fold as a function of salt concentration, detergent, pH, and 2,2,2-trifluoro-ethanol (TFE); only the addition of TFE resulted in a structural change. The effect of TFE addition was studied by circular dichroism, structural, and dynamic data obtained by NMR. The data indicate that C82 can adopt an alpha-helical structure; this conformation is likely relevant to one of the functional roles of the HCV Core protein.
Duvignaud
Jean-Baptiste
JB
PROTEO and Department of Biochemistry and Microbiology, Pavillon C-E MARCHAND, Universite Laval, 1030 avenue de Medecine, Local 3255, Quebec, QC G1V 0A6, Canada. jean-baptiste.duvignaud.1@ulaval.ca
Leclerc
Denis
D
Gagné
Stéphane M
SM
D003902:Detergents / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation / Q000187:drug effects; D014270:Trifluoroethanol / Q000494:pharmacology*; D014758:Viral Core Proteins / Q000737:chemistry* / Q000302:isolation & purification
D003902:Detergents; D014758:Viral Core Proteins; C069130:nucleocapsid protein, Hepatitis C virus; D014270:Trifluoroethanol