A MOLECULAR DYNAMICS STUDY ON DES-HEPTAPEPTIDE INSULIN
去七肽胰岛素的分子动力学研究

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.