Unveiling the role of histidine and tyrosine residues on the conformation of the avian prion hexarepeat domain (Articolo in rivista)

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Label
  • Unveiling the role of histidine and tyrosine residues on the conformation of the avian prion hexarepeat domain (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp710702q (literal)
Alternative label
  • Adriana Pietropaolo1; Luca Muccioli1; Claudio Zannoni1; Diego La Mendola2; Giuseppe Maccarrone3; Giuseppe Pappalardo2; Enrico Rizzarelli2,3 (2008)
    Unveiling the role of histidine and tyrosine residues on the conformation of the avian prion hexarepeat domain
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Adriana Pietropaolo1; Luca Muccioli1; Claudio Zannoni1; Diego La Mendola2; Giuseppe Maccarrone3; Giuseppe Pappalardo2; Enrico Rizzarelli2,3 (literal)
Pagina inizio
  • 5182 (literal)
Pagina fine
  • 5188 (literal)
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  • 112 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 16 (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 Dipartimento di Chimica Fisica e Inorganica and INSTM, UniVersita` di Bologna, Viale Risorgimento 4, 40136 Bologna, Italy 2 CNR-Istituto di Biostrutture e Bioimmagini Catania, Viale Andrea Doria 6, 95125 Catania, Italy 3 Dipartimento di Scienze Chimiche, UniVersita` di Catania, Viale Andrea Doria 6, 95125 Catania, Italy (literal)
Titolo
  • Unveiling the role of histidine and tyrosine residues on the conformation of the avian prion hexarepeat domain (literal)
Abstract
  • The prion protein (PrPC) is a glycoprotein that in mammals, differently from avians, can lead to prion diseases, by misfolding into a â-sheet-rich pathogenic isoform (PrPSc). Mammal and avian proteins show different N-terminal tandem repeats: PHGGGWGQ and PHNPGY, both containing histidine, whereas tyrosine is included only in the primary sequence of the avian protein. Here, by means of potentiometric, circular dichroism (CD), and molecular dynamics (MD) studies at different pH values, we have investigated the conformation of the avian tetrahexarepeat (PHNPGY)4 (TetraHexaPY) with both N- and C-termini blocked by acetylation and amidation, respectively. We have found, also with the help of a recently proposed protein chirality indicator (Pietropaolo, A.; Muccioli, L.; Berardi, R.; Zannoni, C. Proteins 2008, 70, 667-677), a conformational dependence on the protonation states of histidine and tyrosine residues: the turn formation is pH driven, and at physiological pH a pivotal role is played by the tyrosine OH groups which give rise to a very compact bent structure of backbone upon forming a hydrogen-bond network. (literal)
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