http://www.cnr.it/ontology/cnr/individuo/prodotto/ID204382
NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41 (Articolo in rivista)
- Type
- Label
- NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41 (Articolo in rivista) (literal)
- Anno
- 1996-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/(SICI)1097-0282(199603)38:3<423::AID-BIP13>3.0.CO;2-D (literal)
- Alternative label
Consonni, R; Limiroli, R; Longhi, R; Manera, E; Vecchio, G; Ragona, L; Siccardi, AG; Zetta, L (1996)
NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Consonni, R; Limiroli, R; Longhi, R; Manera, E; Vecchio, G; Ragona, L; Siccardi, AG; Zetta, L (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0282(199603)38:3%3C423::AID-BIP13%3E3.0.CO;2-D/pdf (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Consonni, R; Limiroli, R; Ragona, L; Zetta, L ISMAC Milano
Longhi, R; Manera, E; Vecchio, G; ICRM MIlano (literal)
- Titolo
- NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41 (literal)
- Abstract
- CD and nmr characterizations are reported for the 23-mer peptide CMC;I, corresponding to residues 577-599 of gp41, the transmembrane glycoplotein of the human immunodeficiency virus I. Concentration, temperature, and pH dependencies of CD and nmr spectra are indicative of self-association with a consequent stabilization of secondary structural elements in water. The addition to the water solution of small amounts of trifluoroethanol induces a secondary structure, mostly due to the presence of helical elements. The amphipathic character of the helix and the presence of three hydrophobic 4/3 heptad repeats suggest that the peptide could be structured in a symmetric association of helices, such as in a coiled-coil structure. This behavior is discussed in terms of a possible role of this segment in the gp41 envelope oligomerization. (literal)
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