Abstract
To study the intrinsic structural properties of three 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.
Keywords: Prion, helix stability, helix propensity, molecular dynamics, helical peptides
Protein & Peptide Letters
Title: Human Prion Protein Helices: Studying Their Stability by Molecular Dynamics Simulations (SUPPLEMENTARY MATERIAL)
Volume: 16 Issue: 9
Author(s): Susan Costantini and Angelo M. Facchiano
Affiliation:
Keywords: Prion, helix stability, helix propensity, molecular dynamics, helical peptides
Abstract: To study the intrinsic structural properties of three 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.
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Cite this article as:
Costantini Susan and Facchiano M. Angelo, Human Prion Protein Helices: Studying Their Stability by Molecular Dynamics Simulations (SUPPLEMENTARY MATERIAL), Protein & Peptide Letters 2009; 16 (9) . https://dx.doi.org/10.2174/092986609789055313
DOI https://dx.doi.org/10.2174/092986609789055313 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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