Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals(282 views visite) Pietropaolo A, Muccioli L, Zannoni C, Rizzarelli E
Dipartimento di Chimica Fisica ed Inorganica and INSTM, Universita di Bologna, V.le Risorgimento, 4, I-40136 Bologna, Italy. Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 1-95125 Catania, Italy
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Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals
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 chirality 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 beta-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.
Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals
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