MOLECULAR-DYNAMICS SIMULATION OF THE STABILITY OF A 22-RESIDUE ALPHA-HELIX IN WATER AND 30-PERCENT TRIFLUOROETHANOL

被引:94
作者
VANBUUREN, AR [1 ]
BERENDSEN, HJC [1 ]
机构
[1] UNIV GRONINGEN,BIOPHYS CHEM LAB,9747 AG GRONINGEN,NETHERLANDS
关键词
D O I
10.1002/bip.360330802
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
A molecular dynamics (MD) simulation was performed on the alpha-helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical right-handed alpha-helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. (C) 1993 John Wiley & Sons, Inc.
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页码:1159 / 1166
页数:8
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