SOLUTION CONFORMATION OF A PEPTIDE CORRESPONDING TO RESIDUES-151-172 OF HIV-1 INTEGRASE USING NMR AND CD SPECTROSCOPY

Citation
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
Citations number
36
Categorie Soggetti
Biology
ISSN journal
03678377
Volume
47
Issue
1-2
Year of publication
1996
Pages
117 - 122
Database
ISI
SICI code
0367-8377(1996)47:1-2<117:SCOAPC>2.0.ZU;2-6
Abstract
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.