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 |
Journal | FEBS Lett |
Volume | 374 |
Issue | 1 |
Pagination | 117-21 |
Date Published | 1995 Oct 23 |
ISSN | 0014-5793 |
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 |
Abstract | 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. |
PubMed ID | 7589496 |
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