Jw. Cheng et al., SOLUTION CONFORMATION OF A PEPTIDE CORRESPONDING TO RESIDUES-151-172 OF HIV-1 INTEGRASE USING NMR AND CD SPECTROSCOPY, International journal of peptide & protein research, 47(1-2), 1996, pp. 117-122
The solution structure of a synthetic peptide corresponding to residue
s 151-172 of HIV-1 integrase has been determined by NMR and CD spectro
scopy. Residues 151-172 of HIV-1 integrase were predicted to be an cc-
helix and to be responsible for the oligomerization of HIV-1 integrase
. Two-dimensional H-1 NMR and CD studies indicate that this synthetic
peptide adopts an amphipathic alpha-helical conformation in TFE-contai
ning solution. However, concentration-dependent CD studies reveal that
this peptide motif does not form dimers or oligomers in solution as p
redicted. These results are in agreement with the crystal structure of
the catalytic domain of HIV-1 integrase reported recently. (C) Munksg
aard 1996.