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Titolo:
CONFORMATIONAL FEATURES OF A SYNTHETIC CYCLIC PEPTIDE CORRESPONDING TO THE COMPLETE V3 LOOP OF THE RF HIV-1 STRAIN IN WATER AND WATER TRIFLUOROETHANOL SOLUTIONS/
Autore:
VRANKEN WF; BUDESINSKY M; MARTINS JC; FANT F; BOULEZ K; GRASMASSE H; BORREMANS FAM;
Indirizzi:
STATE UNIV GHENT,DEPT ORGAN CHEM,BIOMOL NMR UNIT,KRIJGSLAAN 281,S4 BIS B-9000 GHENT BELGIUM STATE UNIV GHENT,DEPT ORGAN CHEM,BIOMOL NMR UNIT B-9000 GHENT BELGIUM ACAD SCI CZECH REPUBL,INST ORGAN CHEM & BIOCHEM PRAGUE CZECH REPUBLIC INST PASTEUR F-59019 LILLE FRANCE
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 236, anno: 1996,
pagine: 100 - 108
SICI:
0014-2956(1996)236:1<100:CFOASC>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; PRINCIPAL NEUTRALIZING DETERMINANT; ENVELOPE GLYCOPROTEIN GP120; PROTEIN SECONDARY STRUCTURE; NUCLEAR-MAGNETIC-RESONANCE; CIRCULAR-DICHROISM SPECTRA; NMR-SPECTRA; HYDROPHOBIC MOMENT; DOMAIN; CELLS;
Keywords:
NMR; CD; RF V3 LOOP; AMPHIPATHIC HELIX; HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
W.F. Vranken et al., "CONFORMATIONAL FEATURES OF A SYNTHETIC CYCLIC PEPTIDE CORRESPONDING TO THE COMPLETE V3 LOOP OF THE RF HIV-1 STRAIN IN WATER AND WATER TRIFLUOROETHANOL SOLUTIONS/", European journal of biochemistry, 236(1), 1996, pp. 100-108

Abstract

The disulfide-bridge-closed cyclic peptide corresponding to the wholeV3 loop of the RF HIV-1 strain was examined by proton two-dimensionalNMR spectroscopy in water and water/trifluoroethanol solutions, Although most of the peptide is conformationally averaged in water, the NOEdata support a beta-turn conformation for the central conservative GPGR region and the presence of nascent helix. Upon addition of trifluoroethanol, helix formation in the C-terminal part becomes apparent. This is confirmed by CD data. NOEs indicative of multiple and transient beta-turns around the Asn6 glycosylation site and NOEs fitting X-ray data on a linear V3 peptide-Fab complex also emerge. The C-terminal helix is shown to have amphipathic character and might thus assist in the infection process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 20:01:09