How conformational transition depends on hydrophobicity of elastin-like polypeptides

被引：0
|
作者：
H. Arkin
M. Bilsel
机构：
[1] Ankara University,Department of Physics Engineering
来源：
The European Physical Journal E | 2010年 / 31卷
关键词：
Monte Carlo; Conformational Transition; Ramachandran Plot; Fourth Position; Secondary Structure Formation;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The three-dimensional structures of elastin-like polypeptides Val1-Pro2-Gly3-Xaa4-Gly5 were investigated by using the multicanonical Monte Carlo (MC) simulation procedure. By substituting different amino acids in the fourth position of the sequence, the thermodynamical variables are calculated in vacuo and in solvent to determine the hydrophobicity dependence of the conformational transition temperatures of the peptides. Resultant hydrophobicity scale is in good agreement with many hydrophobicity scales.
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页码：327 / 332
页数：5
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