去七肽胰岛素的分子动力学研究

本文用分子动力学的方法对去七肽胰岛素(DHPI)分子的构象进行了研究,首先用分子动力学方法对晶体胰岛素分子的构象能进行了优化,然后除去B链C端的最后七个残基(B24—B30),做分子动力学模拟,得到了DHPI的平衡构象和均方差波动。胰岛素分子的X射线晶体衍射结构和能量优化构象之间的均方根偏差为0.1;所得DHPI构象和胰岛素能量优化构象间C原子间的均方根偏差为1.8。变化最大的区域是A8—A10,A18—A21,B1—B41和B18—B23。

A MOLECULAR DYNAMICS STUDY ON DES-HEPTAPEPTIDE INSULIN

A molecular dynamics study on des-hcptapeptide insulin conformation has been carried out. The energy of the conformation of insulin has been minimized using molecular dynamics method, the cnergy-refined conformation of insulin is obtained. Then the last seven residues in the C-terminal of the B-chain (B24-B30) are removed, a molecular dynamics simulation has been carried out. The equilibrium conformation and r. m. s. fluctuation of des-heptapeptide insulin (DHPI) are obtained. The r.m.s. deviation of all atoms between the X-ray-structure and energy-refined conformation of insulin is 0.1 A. The r.m.s. deviation of C atoms between the obtained DHPI conformation and the energy-refined conformation of insulin is 1.8 A. The largest change happened in A8-A10, A18-A21, B1-B4, B18-B23.