Molecular dynamics simulations of a winter flounder "antifreeze" polypeptide in aqueous solution.
Molecular dynamics simulations of a winter flounder "antifreeze" polypeptide in aqueous solution.
复制标题
水溶液中冬鲽“防冻”多肽的分子动力学模拟。
DOI：
10.1002/bip.360331002
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发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Clancy,P
中科院分区：
文献类型：
--
作者：
McDonald,SM;Brady,JW;Clancy,P
利用分子动力学计算机模拟技术研究了一种冬季比目鱼防冻多肽（HPLC‐6）在真空和水溶液中的含量。该多肽的螺旋构象在真空和溶液中都是稳定的。主要的稳定相互作用是主链氢键、盐桥相互作用和溶质-溶剂氢键。在真空和300 K溶剂中均观察到多肽链中部明显弯曲。讨论了引起弯曲的可能原因。通过对突变多肽分子在真空中的模拟，我们得出结论，天然多肽的弯曲是由涉及Thr 24侧链的侧链与主氢键竞争引起的，并由Lys 18‐Glu 22盐桥引起的螺旋上的应变促进。©1993 John Wiley & Sons, Inc
A winter flounder antifreeze polypeptide (HPLC‐6) has been studied in vacuo and in aqueous solution using molecular dynamics computer simulation techniques. The helical conformation of this polypeptide was found to be stable both in vacuum and in solution. The major stabilizing interactions were found to be the main‐chain hydrogen bonds, a salt‐bridge interaction, and solute–solvent hydrogen bonds. A significant bending in the middle of the polypeptide chain was observed both in vacuo and in solvent at 300 K. Possible causes of the bending are discussed. From simulations of mutant polypeptide molecules in vacuo, it is concluded that the bend in the native polypeptide was caused by side chain to backbone hydrogen bond competition involving the Thr 24 side chain and facilitated by strains on the helix resulting from the Lys 18‐Glu 22 salt bridge. © 1993 John Wiley & Sons, Inc.