Abstract
The solution structure of a synthetic peptide corresponding to residues 151-172 of HIV-1 integrase has been determined by NMR and CD spectroscopy. Residues 151-172 of HIV-1 integrase were predicted to be an α-helix and to be responsible for the oligomerization of HIV-1 integrase. Two-dimensional 1 H NMR and CD studies indicate that this synthetic peptide adopts an amphipathic α-helical conformation in TFE-containing solution. However concentration-dependent CD studies reveal that this peptide motif does not form dimers or oligomers in solution as predicted. These results are in agreement with the crystal structure of the catalytic domain of HIV-1 integrase reported recently.