Folding of a 16-residue helical peptide using molecular dynamics simulation with Tsallis effective potential
Folding of a 16-residue helical peptide using molecular dynamics simulation with Tsallis effective potential
复制标题
使用 Tsallis 有效势的分子动力学模拟折叠 16 个残基螺旋肽
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
Shaomeng Wang
中科院分区：
文献类型：
--
作者：
Youngshang Pak;Shaomeng Wang
我们已经证明，分子动力学模拟方法与 Tsallis 有效势相结合，能够使 16 个残基模型肽在相当短的时间内折叠成完整的 α 螺旋。目前的研究还表明，利用该方法实际上可以观察到肽的可逆折叠，这主要是由于其克服势能垒的卓越能力。因此，预计新方法可以为蛋白质和DNA等多自由度系统提供非常有效的构象搜索工具。
We have demonstrated that a molecular dynamics simulation method in conjunction with a Tsallis effective potential enables a 16-residue model peptide to fold into a complete α-helix in a reasonably short time. The current study also indicates that one can practically observe reversible foldings of the peptide with the method, mainly due to its superior capability of overcoming potential energy barriers. Therefore it is anticipated that the new method may provide a quite efficient conformational searching tool for systems with many degrees of freedom such as proteins and DNAs.
影响因子：
2.9
作者：
SCHOLTZ, JM;QIAN, H;BALDWIN, RL
通讯作者：
BALDWIN, RL