The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution

W F Vranken, M Budesinsky, F Fant, K Boulez, F A Borremans

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

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 languageEnglish
Pages (from-to)117-121
Number of pages5
JournalFEBS Letters
Volume374
Issue number1
Publication statusPublished - 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

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