@prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . @prefix prodotto: . unitaDiPersonaleInterno:MATRICOLA29183 pubblicazioni:autoreCNRDi prodotto:ID168884 . unitaDiPersonaleInterno:MATRICOLA19927 pubblicazioni:autoreCNRDi prodotto:ID168884 . @prefix prodottidellaricerca: . @prefix istituto: . istituto:CDS017 prodottidellaricerca:prodotto prodotto:ID168884 . istituto:CDS019 prodottidellaricerca:prodotto prodotto:ID168884 . @prefix rdf: . prodotto:ID168884 rdf:type prodotto:TIPO1101 . @prefix retescientifica: . prodotto:ID168884 rdf:type retescientifica:ProdottoDellaRicerca . @prefix rdfs: . prodotto:ID168884 rdfs:label "Folding of peptides characterized by c3Val, a highly constrained analog of valine (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID168884 pubblicazioni:anno "2003-01-01T00:00:00+01:00"^^xsd:gYear . @prefix skos: . prodotto:ID168884 skos:altLabel "
Peggion C., Formaggio F., Crisma M., Toniolo C., Jim\u00E9nez A.I., Cativiela C., Kaptein B., Broxterman Q.B., Saviano M., Benedetti E. (2003)
Folding of peptides characterized by c3Val, a highly constrained analog of valine
in Biopolymers (Print)
"^^rdf:HTML ; pubblicazioni:autori "Peggion C., Formaggio F., Crisma M., Toniolo C., Jim\u00E9nez A.I., Cativiela C., Kaptein B., Broxterman Q.B., Saviano M., Benedetti E."^^xsd:string ; pubblicazioni:paginaInizio "178"^^xsd:string ; pubblicazioni:paginaFine "191"^^xsd:string ; pubblicazioni:numeroVolume "68"^^xsd:string . @prefix ns10: . prodotto:ID168884 pubblicazioni:rivista ns10:ID392898 ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:titolo "Folding of peptides characterized by c3Val, a highly constrained analog of valine"^^xsd:string ; prodottidellaricerca:abstract "Using a combined chemical/chiral chromatographic approach we synthesized an N-protected derivative of (R)-c(3)Val, a severely conformationally restricted C-alpha-tetrasubstituted alpha-amino acid characterized by a C-beta,C-beta-dimethylated cyclopropane system. A set of terminally protected derivatives and model peptides (to the heptamer level), containing one or two (R)-c(3)Val residues in combination with either Aib or Gly residues, was prepared by solution methods. A detailed solution and crystal-state conformational investigation, based on Fourier transform infrared (FTIR) absorption, H-1-NMR, and x-ray diffraction techniques, performed in comparison with a similar study on related derivatives and peptides rich in (alphaMe)Val, the prototype of C-alpha-tetrasubstituted alpha-amino acids of this subfamily, allowed us to conclude the following: (a) c(3)Val is a good beta-bend and helix former, although less efficient than (alphaMe)Val. (b) The relationship between alpha-carbon chirality and screw sense of the folded structure formed is the same as that of (alphaMe) Val, i.e., the (R)-enantiomer has a strong left-handed bias. (c) c(3)Val seems more prone than (alphaMe)Val to fold into a gamma-bend conformation. The conformational propensities of C-beta,C-beta-disubstituted Ac(3)c residues are also discussed in comparison with those of the parent cyclopropane residue." ; prodottidellaricerca:prodottoDi istituto:CDS019 , istituto:CDS017 ; pubblicazioni:autoreCNR unitaDiPersonaleInterno:MATRICOLA19927 , unitaDiPersonaleInterno:MATRICOLA29183 . ns10:ID392898 pubblicazioni:rivistaDi prodotto:ID168884 .