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1996-02-26
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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).