Document 0629
 DOCN  M9620629
 TI    The complete Consensus V3 loop peptide of the envelope protein gp120 of
       HIV-1 shows pronounced helical character in solution.
 DT    9602
 AU    Vranken WF; Budesinsky M; Fant F; Boulez K; Borremans FA; Department of
       Organic Chemistry, University of Gent, Belgium.
 SO    FEBS Lett. 1995 Oct 23;374(1):117-21. Unique Identifier : AIDSLINE
       MED/96049568
 AB    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.
 DE    Amino Acid Sequence  Consensus Sequence  HIV Envelope Protein
       gp120/*CHEMISTRY  Molecular Sequence Data  Nuclear Magnetic Resonance
       Peptide Fragments/*CHEMISTRY  Protein Conformation  Sequence Alignment
       Solutions  Support, Non-U.S. Gov't  Trifluoroethanol/CHEMISTRY
       Water/CHEMISTRY  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).