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.
Original language | English |
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Pages (from-to) | 117-121 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 374 |
Issue number | 1 |
Publication status | Published - 1995 |
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