Human Prion Protein Helices: Studying Their Stability by Molecular Dynamics Simulations

被引:3
|
作者
Costantini, Susan [1 ,2 ,3 ]
Facchiano, Angelo M. [1 ,2 ]
机构
[1] CNR, Inst Food Sci, Lab Bioinformat & Computat Biol, I-83100 Avellino, Italy
[2] Univ Naples 2, CRISCEB, I-80138 Naples, Italy
[3] CROM Fiorentino Lo Vuolo, I-83013 Mercogliano, Italy
来源
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 09期
关键词
Prion; helix stability; helix propensity; molecular dynamics; helical peptides; FOLDING PROBLEM; STABILIZATION; DETERMINANTS; PARAMETERS; INSIGHTS; BINDING;
D O I
10.2174/092986609789055313
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1057 / 1062
页数:6
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