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

TitleThe complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.
Publication TypeJournal Article
Year of Publication1995
AuthorsVranken, W. F., M. Budesinsky, F. Fant, K. Boulez, and F. A. Borremans
JournalFEBS Lett
Volume374
Issue1
Pagination117-21
Date Published1995 Oct 23
ISSN0014-5793
KeywordsAmino 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 JournalFEBS Lett.
PubMed ID7589496
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