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An NMR and molecular dynamics investigation of the avian prion hexarepeat conformational features in solution (119 visite)

Pietropaolo A, Raiola L, Muccioli L, Tiberio G, Zannoni C, Fattorusso R, Isernia C, La Mendola D, Pappalardo G, Rizzarelli E

Chemical Physics Letters (ISSN: 0009-2614), 2007 Jul 6; 442(1-3): 110-118.

Tipo di articolo: Journal Article, , Impact factor: 2.207, Impact factor a 5 anni: 2.392, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-34250637939&partnerID=40&md5=137c6dcff0c690500285ea460dc650c8

Parole chiave: Conformations, Copper, Glycoproteins, Mammals, Molecular Dynamics, Nuclear Magnetic Resonance, Pathogens, Avian Hexarepeat, Copper Binding Glycoprotein, Prion Diseases,

Affiliazioni: *** IBB - CNR ***
Dipartimento di Chimica Fisica e Inorganica, Università di Bologna, INSTM, v.le Risorgimento 4, 40136 Bologna, Italy
Dipartimento di Scienze Ambientali, Seconda Università di Napoli, via Vivaldi 43, 81100 Caserta, Italy
CNR-Istituto di Biostrutture e Bioimmagini Catania, v.le A. Doria 6, 95125 Catania, Italy


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The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and molecular dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions. (C) 2007 Elsevier B.V. All rights reserved.
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Saviano M, Rossi F, Pavone V, Di Blasio B, Pedone C
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Tancredi T, Zanotti G, Rossi F, Benedetti E, Pedone C, Temussi PA
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