beta 2-Strand of salivary S cystatins: A \"chemeleon sequence\" (Articolo in rivista)

Type
Label
  • beta 2-Strand of salivary S cystatins: A \"chemeleon sequence\" (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbrc.2009.06.105 (literal)
Alternative label
  • Alberto Vitali; Cristiana Carelli Alinovi; Maria Cristina De Rosa; Raffaele Petruzzelli (2009)
    beta 2-Strand of salivary S cystatins: A "chemeleon sequence"
    in Biochemical and biophysical research communications (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Alberto Vitali; Cristiana Carelli Alinovi; Maria Cristina De Rosa; Raffaele Petruzzelli (literal)
Pagina inizio
  • 47 (literal)
Pagina fine
  • 51 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 387 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 5 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biochimica e Biochimica Clinica, Facolt√† di Medicina, Universit√† Cattolica e/o Istituto per la Chimica del Riconoscimento Molecolare, C.N.R., Largo F. Vito 1, 00168 Roma, Italy; Dipartimento di Scienze Biomediche, Universit√† degli Studi ''G. D'Annunzio\", Via dei Vestini 29, 66013 Chieti, Italy (literal)
Titolo
  • beta 2-Strand of salivary S cystatins: A \"chemeleon sequence\" (literal)
Abstract
  • Secondary structure prediction of salivary cystatins S, SA, and SN carried out by several methods label the 39-58 sequence (beta2-strand) as predominantly a-helical. The helical propensity of a peptide corresponding to beta2-strand of salivary SA cystatin analyzed by CD display high helical propensity in aqueous solution, whereas peptides matching the beta2-strand amino acid sequence of cystatins S and SN, display random coil conformation in aqueous solution but acquire alpha-helical conformation in the presence of trifluoroethanol (TFE). Moreover molecular dynamics simulation performed on the homology modeling of cystatin SA constructed on the basis of recently determined three-dimensional structure of salivary cystatin D, suggests that cystatin SA does not significantly deviate from the starting structure over the course of the simulation. The results obtained indicate that the b2-strand of salivary S cystatins has high helical propensity when isolated from native protein and acquire the final beta structure by interaction with the rest of the polypeptide chain. (literal)
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