1. An NMR and molecular dynamics investigation of the avian prion hexarepeat conformational features in solution
- Author
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Pietropaolo, Adriana, Raiola, Luca, Muccioli, Luca, Tiberio, Giustiniano, Zannoni, Claudio, Fattorusso, Roberto, Isernia, Carla, Mendola, Diego La, Pappalardo, Giuseppe, and Rizzarelli, Enrico
- Subjects
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MOLECULAR dynamics , *DYNAMICS , *HYDROGEN-ion concentration , *BUFFER solutions - Abstract
Abstract: 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. [Copyright &y& Elsevier]
- Published
- 2007
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