THE STUDY ON THE FLEXIBILITY OF INSULIN HEXAMER IN SOLUTION BY MOLECULAR DYNAMICS SIMULATIONS
胰岛素六聚体在水溶液中的构象柔性研究

In order to study the flexibility of insulin hexamer in solution, two 600 ps molecular dynamics (MD) simulations of the protein complex, R-state human insulin hexamer system, were carried out respectively. Through the comparison analysis for two MD simulation data, it was found that for the system with Zn2+ ions and phenol, the conformational flexibility of insulin hexamer was decreased. However, in the absence of Zn2+ and phenol, the insulin hexamer exhibits a higher degree of conformational flexibility in aqueous solution. The remarkable and rapid conformational changes of the β-sheet at C-terminus of the B-chain in every insulin monomer provide a structural basis for insulin to bind with its receptor. These results are in good agreement with the experimental observation.