Role of aspartic acid in collagen structure and stability: A molecular dynamics investigation.
Role of aspartic acid in collagen structure and stability: A molecular dynamics investigation.
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天冬氨酸在胶原蛋白结构和稳定性中的作用：分子动力学研究。
DOI：
10.1021/jp0625715
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
T. Ramasami
中科院分区：
文献类型：
--
作者：
S. S. Raman;R. Parthasarathi;V. Subramanian;T. Ramasami
一个分子动力学（MD）模拟研究已经进行了了解三螺旋胶原模型的稳定性。计算结果表明，天冬氨酸残基在不同位置的存在下，导致在结构的局部变化。对分子动力学模拟过程中的均方根偏差（RMSD）、径向分布函数（RDF）、起皱效应、二面角变化、氢键（H-键）和构象变化的分析表明，序列中的局部扰动、由于天冬氨酸去除胶原中的五元环而增加的链柔性、分子间H-键模式的改变水缔合的差异主要影响天冬氨酸对胶原的稳定性。
A molecular dynamics (MD) simulation study has been carried out to understand the stability of the triple helical collagen models. The calculations show that the presence of the aspartic acid residue in different positions leads to the local variation in the structure. Analyses of root-mean-square deviation (RMSD), radial distribution function (RDF), puckering effect, dihedral angle variation, hydrogen bond (H-bond), and conformational changes during molecular dynamics simulation reveal that the local perturbation in the sequences, increase in chain flexibility due to removal of five membered rings in the collagen by aspartic acid, change of intermolecular H-bonding pattern, and differences in the association of water are mainly influencing the nature of stabilization of collagen by aspartic acid.