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Human Prion Protein Helices: Studying Their Stability by Molecular Dynamics Simulations (SUPPLEMENTARY MATERIAL)

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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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Keywords: Prion; helical peptides; helix propensity; helix stability; molecular dynamics

Document Type: Research Article

Publication date: September 1, 2009

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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