由盐浓度驱动的载脂蛋白A1的折叠作为改善胆固醇捕获的可能机制
Folding of the apolipoprotein A1 driven by the salt concentration as a possible mechanism to improve cholesterol trapping
摘要：
利用原子级详细的分子动力学模拟研究了离子强度增加时胆固醇捕获载脂蛋白A1在水溶液中的折叠。我们计算了各种结构性质来表征蛋白质的构象，如回转半径，径向分布函数和端到端距离。此外，我们使用专门为蛋白质表征定制的工具报告信息，例如平均最小距离矩阵和Ramachandran图。我们发现，这种蛋白质的两种不同的配置是优选的，一个是蛋白质的延伸，和一个它形成环或封闭结构。有人认为，后者促进了蛋白质与胆固醇和其他脂肪酸的结合。
英文摘要：
The folding of the cholesterol trapping apolipoprotein A1 in aqueous solution at increasing ionic strength is studied using atomically detailed molecular dynamics simulations. We calculate various structural properties to characterize the conformation of the protein, such as the radius of gyration, the radial distribution function and the end to end distance. Additionally we report information using tools specifically tailored for the characterization of proteins, such as the mean smallest distance matrix and the Ramachandran plot. We find that two qualitatively different configurations of this protein are preferred, one where the protein is extended, and one where it forms loops or closed structures. It is argued that the latter promote the association of the protein with cholesterol and other fatty acids.
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