Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals (Articolo in rivista)

Type
Label
  • Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/cphc.200900078 (literal)
Alternative label
  • Rizzarelli, Enrico (1); Zannoni, Claudio (2); Pietropaolo, Adriana (2); Muccioli, Luca (2) (2009)
    Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals
    in ChemPhysChem (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Rizzarelli, Enrico (1); Zannoni, Claudio (2); Pietropaolo, Adriana (2); Muccioli, Luca (2) (literal)
Pagina inizio
  • 1500 (literal)
Pagina fine
  • 1510 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 10 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 9-10 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Dipartimento di Scienze Chimiche - Universit√† di Catania; (2) Dipartimento di Chimica Fisica ed Inorganica and INSTM - Universit√† di Bologna (literal)
Titolo
  • Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals (literal)
Abstract
  • We investigate the conformations of the full chicken prion protein (ChPrP1-267) in solution at neutral pH with molecular dynamics simulations. We focus on the persistence of its secondary structure motifs using a recently proposed protein chirali-ty indicator [A. Pietropaolo et al., Proteins 2008, 70, 667-677]. From this, we find a high rigidity of helix 2 (ChPrP178-195) and of the hexarepeat domain, which is turn rich, and a plasticity of the short ?-sheet, consistent with the available NMR structural details. We also determine the extent of solvation for each residue, revealing local minima for such structured regions. These features hint at a possible origin of the high resistance to proteolysis of the avian prion proteins and of its capability in preventing the aggregation in comparison to mammals. ¬© 2009 Wiley-VCH Verlag. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it