title: Human prion protein helices: studying their stability by molecular dynamics simulations.
abstract: To study the intrinsic structural properties of three in human prion helices and analyse their stability, we conducted molecular dynamics simulations, applied helix propensity predictions and evaluated the energetic contribution of the helical regions to the PrP protein stability. Our results suggest that three helices present different stability and the helix 2 results the least stable.
authors.affiliation: Laboratory of Bioinformatics and Computational Biology, Institute of Food Sciences - CNR, via Roma 52 A/C, 83100 Avellino, Italy.
authors.forename: Susan
authors.initials: S
authors.lastname: Costantini
authors.forename: Angelo M
authors.initials: AM
authors.lastname: Facchiano
mesh_terms: D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D011328:Prions / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D011328:Prions