期刊论文

Roles of removal of disulfide bonds and of protein residues in the stability of Ginkbilobin-2

中文

中南林业科技大学学报

1673-923X

2016

36

10

65-71

10.14067/j.cnki.1673-923x.2016.10.012

国家科技部公益行业专项

本校为第一机构

通过分子动力学模拟,研究了二硫键以及蛋白自身残基在维持蛋白构象稳定中起到的作用,对野生型、截断型和突变型的银杏抗菌蛋白Ginkbilobin-2(Gnk-2)的构象变化进行了分析。结果表明:在100 ns 的模拟时间内,造成蛋白构象发生显著变化的主要原因,是蛋白自身残基的缺失,而短时间内二硫键在维持蛋白结构稳定方面的作用并不明显。仅通过比较短时间内模拟所得到的截断型和野生型蛋白的结构变化无法判断二硫键对蛋白结构稳定性的影响。这与文献中仅通过100 ns 的时间内模拟野生型和截断型蛋白均方根位移(RMSD)值的变化趋势,便判断出二硫键的断裂是引发蛋白构象发生显著变化的主要原因的看法,是不一致的...

Molecular dynamics (MD) simulations were used within a short time of 100 ns to study and compare the conformational changes of the wild type form with the reduced form of the protein, where the cysteine residues that formed the disulfide bonds were removed. However, an important issue is that upon the removal of residues, besides the effect of elimination of disulfide bonds, the removal of residues itself is also expected to affect the protein conformation. To determine which effect plays a critical role in affecting the conformation within the short simulation time, we take the ginkbilobin-2 ...