RESTRAINED AND UNRESTRAINED MOLECULAR-DYNAMICS SIMULATIONS IN THE NVT ENSEMBLE OF ALAMETHICIN
RESTRAINED AND UNRESTRAINED MOLECULAR-DYNAMICS SIMULATIONS IN THE NVT ENSEMBLE OF ALAMETHICIN
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DOI：
10.1002/bip.360301109
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发表时间：
1990-01-01
期刊：
影响因子：
2.9
通讯作者：
FRATERNALI, F
中科院分区：
文献类型：
--
作者：
FRATERNALI, F
已经在NVT样品中对跨膜抗生素肽丙甲霉素进行了分子动力学模拟（即，系统的粒子数N、体积V和温度T保持恒定）。讨论了该分子的结构和构象灵活性的结果，并与以前的实验CD，X-射线，NMR数据和理论计算的碎片类似物进行了比较。一个广泛的研究，从氢键模式分析的结构和动力学性质。根据分子的结构特征和动力学行为，将分子分为三个区域，并描述了三个区域运动之间的相关性。
Molecular dynamics simulations on the transmembrane antibiotic peptide alamethicin have been performed in the NVT ensamble (i.e., the number of particles N, the volume V, and the temperature T of the system are kept constant). Results on the structure and conformational flexibility of this molecule are discussed and compared with previous experimental CD, x-ray, nmr data and theoretical computations on fragments analogues.An extensive study of structural and dynamic properties from H-bonding pattern analysis is presented. Evidences for a largely alpha-helix structure with some extent of freedom in the C-terminal region are found.Further, a partition of the molecule into three regions on the base of structural features and dynamic behavior has been proposed, and the correlation among the motions of the three regions is described.