Premium
Conformational Preferences of the Full Chicken Prion Protein in Solution and Its Differences with Respect to Mammals
Author(s) -
Pietropaolo Adriana,
Muccioli Luca,
Zani Claudio,
Rizzarelli Enrico
Publication year - 2009
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200900078
Subject(s) - prion protein , proteolysis , molecular dynamics , chemistry , chirality (physics) , protein secondary structure , protein structure , prion proteins , attraction , globular protein , protein folding , proteases , crystallography , biophysics , biology , biochemistry , computational chemistry , physics , enzyme , medicine , chiral symmetry breaking , disease , pathology , quantum mechanics , nambu–jona lasinio model , quark , linguistics , philosophy
Chicken nugget: Simulations of the full chicken prion protein (see picture) and chirality analysis provide possible explanations for its resistance to proteases—and for the fold stability of the avian prion globular core. The three alpha helices exhibit different flexibilities and secondary structure propensities.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 β‐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.