Solution conformation of a peptide corresponding to residues 151-172 of HIV-1 integrase using NMR and CD spectroscopy.
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 alpha-helix and to be responsible for the oligomerization of HIV-1 integrase. Two-dimensional 1H NMR and CD studies indicate that this synthetic peptide adopts an amphipathic alpha-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.
Cheng
J W
JW
Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC.
Cheng
C C
CC
Lyu
P C
PC
Chen
S T
ST
Lin
T H
TH
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019427:HIV Integrase / Q000737:chemistry*; D015497:HIV-1; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D016662:Virus Integration
D010446:Peptide Fragments; D012996:Solutions; D019427:HIV Integrase