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Conformational changes of the wild-type hIAPP and the S20P mutant in water revealed by molecular dynamics simulations

机译:分子动力学模拟野生型HIAPP和S20P突变体的构象变化

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Conformational changes of wild-type (WT) hIAPP and the S20P mutant in explicit water are investigated using molecular dynamics. In the whole simulation, WT shows compacter structure and has more hydrogen-bond networks than S20P. The residues 14-18 in WT is always maintained as a helical structure which is stabilized by the hydrogen bond between Ser20 and NH group of His 18, and the other regions in WT partially loosen from a-helix structures into the coil structures. The S20P mutant in a shortage of hydrogen-bond interaction unfolds faster than WT. This work provides insight into the specific conformation of IAPP which is associated with the generation of amyloid fibrils.
机译:利用分子动力学研究了野生型(WT)HIAPP和S20P突变体的构象变化。在整个模拟中,WT显示了Compacter结构,并且具有比S20P更多的氢键网络。 WT中的残基14-18总是保持为螺旋结构,其通过他18的Ser20和NH组之间的氢键稳定,并且WT中的其他区域部分松开在螺旋结构中进入线圈结构。 S20P突变体在短缺氢粘合相互作用的缺乏比wt更快。这项工作提供了洞察IAPP的具体构象,这与产生淀粉样蛋白原纤维的产生相关。

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