Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species (Articolo in rivista)

Type
Label
  • Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1039/b700764g (literal)
Alternative label
  • Danilo Milardi (2); Matteo Pappalardo; (1); Carmelo La Rosa (1); Domenico Grasso (1) (2007)
    Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species
    in New journal of chemistry (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Danilo Milardi (2); Matteo Pappalardo; (1); Carmelo La Rosa (1); Domenico Grasso (1) (literal)
Pagina inizio
  • 901 (literal)
Pagina fine
  • 905 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 31 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Dipartimento di Scienze Chimiche - Universita' di Catania; (2) Istituto di Biostrutture e Bioimmagini CNR-Sezione di Catania (literal)
Titolo
  • Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species (literal)
Abstract
  • Prion diseases are associated with an abnormal conformational transition involving the prion protein and are known to affect mammals. Here, the different mechanical behaviour of two mammalian, human (HuPrP) and Syrian hamster (ShaPrP), and two non-mammalian, chicken (ChPrP) and turtle (TuPrP), prions was assessed by steered molecular dynamics simulations performed on the globular domains of the four proteins. In mammalian prions a greater resistance to external stretching forces and an earlier occurrence of irreversible events were observed. The different unfolding profile of mammalian prions, ascribable to the intramolecular interactions involving helix 1 with helix 3, implicate the existence of metastable non-native states which may prompt abnormal pathways of protein misfolding and aggregation. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


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