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

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

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

• ChemPhysChem (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 - Università di Catania; (2) Dipartimento di Chimica Fisica ed Inorganica and INSTM - Università 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

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• ENRICO RIZZARELLI (Persona)

Insieme di parole chiave

• Keywords of "Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR di

• ENRICO RIZZARELLI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ChemPhysChem (Rivista)

Insieme di parole chiave di

• Keywords of "Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals" (Insieme di parole chiave)