FOLDING SIMULATIONS OF ALANINE-BASED PEPTIDES WITH LYSINE RESIDUES

被引:46
作者
SUNG, SS
机构
[1] Research Institute, Cleveland Clinic Foundation, Ohio
关键词
D O I
10.1016/S0006-3495(95)80259-6
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The folding of short alanine-based peptides with different numbers of lysine residues is simulated at constant temperature (274 K) using the rigid-element Monte Carlo method. The solvent-referenced potential has prevented the multiple-minima problem in helix folding. From various initial structures, the peptides with three lysine residues fold into helix-dominated conformations with the calculated average helicity in the range of 60-80%. The peptide with six lysine residues shows only 8-14% helicity. These results agree well with experimental observations. The intramolecular electrostatic interaction of the charged lysine side chains and their electrostatic hydration destabilize the helical conformations of the peptide with six lysine residues, whereas these effects on the peptides with three lysine residues are small. The simulations provide insight into the helix-folding mechanism, including the beta-bend intermediate in helix initiation, the (i,i + 3) hydrogen bonds, the asymmetrical helix propagation, and the asymmetrical helicities in the N- and C-terminal regions. These findings are consistent with previous studies.
引用
收藏
页码:826 / 834
页数:9
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