J. Phys. IV France 11 (2001) Pr10-233-Pr10-235
Conformational study of HGV-NS3 (440-460) by circular dichroism (CD). Effect of lipophillic derivation on CD spectraN. Rojo1, M.A. Alsina2 and I. Haro1
1 Department of Peptide & Protein Chemistry, IIQAB-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain
2 Department of Physicochemistry, Faculty of Pharmacy, University of Barcelona, Av. Joan XXIII, s/n, 08028 Barcelona, Spain
The present study was undertaken to examine the conformation by Circular Dichroism spectroscopy of the (440-460) : AIAYYRGKDSSIIKDGDLVVC peptide sequence belonging to the non-structural protein (NS3) of hepatitis G virus (HGV). The conformation of free HGV-NS3(440-460) and two lipophilic derivates at the N-terminus with palmitic and miristic acids respectively, was studied at different concentrations in HEPES as well as in the presence of the most commonly used agents for stabilizing conformations (TFE,HFIP).
© EDP Sciences 2001