Molecular dynamics simulations of the unfolding of an alpha-helical analogue of ribonuclease A S-peptide in water.
Molecular dynamics simulations of the unfolding of an alpha-helical analogue of ribonuclease A S-peptide in water.
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DOI：
10.1021/bi00230a009
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发表时间：
1991-04
期刊：
影响因子：
2.9
通讯作者：
J. Tirado-Rives;W. L. Jorgensen
中科院分区：
文献类型：
--
作者：
J. Tirado-Rives;W. L. Jorgensen
s肽类似物AETAAAKFLREHMDS的分子动力学模拟在278 K的水溶液中进行了300 ps，在358 K的两个不同运行中进行了500 ps。结果与实验结果一致，在低温5℃时，螺旋结构稳定，而在85℃时，螺旋结构展开。在低温模拟中，Glu-2和Arg-10之间形成溶剂分离离子对，His-12侧链向α -螺旋的C端重新取向。高温下展开途径的详细分析也表明，主链螺旋氢键的形成或消失经常通过α平衡与3（10）平衡而无氢键序列发生。
Molecular dynamics simulations of the S-peptide analogue AETAAAKFLREHMDS have been conducted in aqueous solution for 300 ps at 278 K and for 500 ps in two different runs at 358 K. The results show agreement with experimental observations in that at low temperature, 5 degrees C, the helix is stable, while unfolding is observed at 85 degrees C. In the low-temperature simulation a solvent-separated ion pair was formed between Glu-2 and Arg-10, and the side chain of His-12 reoriented toward the C-terminal end of the alpha-helix. Detailed analyses of the unfolding pathways at high temperature have also revealed that the formation or disappearance of main-chain helical hydrogen bonds occurs frequently through an alpha in equilibrium with 3(10) in equilibrium with no hydrogen bond sequence.