|Title||The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.|
|Publication Type||Journal Article|
|Year of Publication||1995|
|Authors||Vranken, W. F., M. Budesinsky, F. Fant, K. Boulez, and F. A. Borremans|
|Date Published||1995 Oct 23|
|Keywords||Amino Acid Sequence, Consensus Sequence, HIV Envelope Protein gp120, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Sequence Alignment, Solutions, Trifluoroethanol, Water|
The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20% trifluoroethanol/water solution. In water, NOE data support a beta-turn conformation for the central conservative GPGR region and point towards partial formation of a helix in the C-terminal part. Upon addition of trifluoroethanol, a C-terminal helix is formed. This is evidenced by NOE data, alpha-proton chemical shift changes and changes in the JN alpha vicinal coupling constants. The C-terminal helix is amphipathic and also occurs in other examined strains. It could therefore be an important feature for the functioning of the V3 loop.
|Alternate Journal||FEBS Lett.|
The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.