Conformational behaviour of an analogue of the S-peptide: A molecular dynamics study

被引：0
|
作者：
Abruscato, V
Ranghino, G
Villa, AM
机构：
[1] IST GUIDO DONEGANI SPA,ENICHEM,I-28100 NOVARA,ITALY
[2] UNIV MILAN,IST CHIM FARMACEUT & TOSSICOL,I-20131 MILAN,ITALY
来源：
PROTEIN AND PEPTIDE LETTERS | 1996年 / 3卷 / 04期
关键词：
D O I：
暂无
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：
The S-peptide, derived from the hydrolysis of Ribonuclease, is a stable alpha-helix in water, although it is only 20 amino acids long. In view of increasing the helical content and stability, a mutated sequence has been proposed. The present work aims to shed light on the conformational preferences and on the helix stability of the proposed sequence by means of Molecular Dynamics simulations performed with different procedures.
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页码：275 / 282
页数：8
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