Theoretical evidence for destabilization of an .alpha.-helix by water insertion: molecular dynamics of hydrated decaalanine
Theoretical evidence for destabilization of an .alpha.-helix by water insertion: molecular dynamics of hydrated decaalanine
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水插入导致 α-螺旋不稳定的理论证据：水合十丙氨酸的分子动力学
DOI：
10.1021/ja00175a004
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发表时间：
1990
影响因子：
15
通讯作者：
D. Beveridge
中科院分区：
文献类型：
--
作者：
F. DiCapua;S. Swaminathan;D. Beveridge
在周期性边界条件下，对水合十肽Ala 10.550H2O进行了分子动力学（MD）模拟.该肽的初始构型是典型的右手α-螺旋。在MD轨迹的过程中，螺旋总体上完好无损且动态稳定，除了观察到初始螺旋不稳定的一个位置之外。在这个位置的螺旋氢键是第一次不稳定的瞬时为100 ps。大约35 ps后，发生了持续的不稳定
A molecular dynamics (MD) simulation was performed on the hydrated decapeptide Ala 10 .550H 2 O under periodic boundary conditions. The initial configuration of the peptide was a canonical right-handed α-helix. Over the course of the MD trajectory, the helix is overall intact and dynamically stable, except for one position in which incipient helix destabilization is observed. The helix hydrogen bond at this position was first destabilized transiently for ∼10 ps. Some 35 ps later, a persistent destabilization occurred