一种高度结构化的β-发夹肽及其单突变体的自由能景观。
Free energy landscapes of a highly structured beta-hairpin peptide and its single mutant.
作者信息
Kim Eunae, Yang Changwon, Jang Soonmin, Pak Youngshang
机构信息
Department of Chemistry, Pusan National University, Busan 609-735, KoreaDepartment of Chemistry, Sejong University, Seoul 143-747, Korea.
出版信息
J Chem Phys. 2008 Oct 28;129(16):165104. doi: 10.1063/1.3000009.
We investigated the free energy landscapes of a highly structured beta-hairpin peptide (MBH12) and a less structured peptide with a single mutation of Tyr6 to Asp6 (MBH10). For the free energy mapping, starting from an extended conformation, the replica exchange molecular dynamic simulations for two beta-hairpins were performed using a modified version of an all-atom force field employing an implicit solvation (param99MOD5/GBSA). With the present simulation approach, we demonstrated that detailed stability changes associated with the sequence modification from MBH12 to MBH10 are quantitatively well predicted at the all-atom level.
我们研究了一种高度结构化的β-发夹肽（MBH12）和一种结构较松散的肽（Tyr6突变为Asp6的MBH10）的自由能景观。为了进行自由能映射，从伸展构象开始，使用采用隐式溶剂化的全原子力场的修改版本（param99MOD5/GBSA）对两种β-发夹进行了副本交换分子动力学模拟。通过目前的模拟方法，我们证明了在全原子水平上可以很好地定量预测与从MBH12到MBH10的序列修饰相关的详细稳定性变化。
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