Molecular Dynamics Simulation Study Of Human Voltage Dependent Anion-selective Channel I In Electric Field

The relationship between structure and function of proteins is essential and fundamental to life science and medical science. Thank to the advance of theories in chemistry and physics, we could know better about protein structure and function, also the relationship between them. Nowadays, the dominant point of view is that protein molecules are flexible and dynamical entities, which is crucial for playing their physiological roles. These conformational change and dynamics are involved in nearly all biological process, such as enzymatic catalysis, molecular recognition, and so on. With the development of modeling approach and the improvement of computational power, molecular dynamics simulation method provide a powerful tool to understand the internal dynamic properties of biomacromolecules. It has been widely used to study various kinds of molecules and recognized as an important way to perform experiments in silica. Meanwhile, molecular dynamics simulation makes it possible to study important molecules which are hard to experiment on.In this article, the author built a heterogeneous system consisting of a protein molecule, lipid molecules and water molecules. Then, the author studied the effects of additional electric field on human voltage dependent anion-selective channel I (hVDAC1). In the simulation, hVDAC1 molecule didn't show any electric field specific motion mode or conformational change. The dominant mode of motion was the horizontal movement of N-terminal helix part in the beta-barrel of hVDAC1. Comparison of trajectories in different electric fields indicated that the direction of electric field was not relevant to any specific motional or conformational change. Considering published physiological experiment results and computational analysis, the author speculated that the adopted crystal structure in this study may not be the same with the structure of VDAC in physiological experiments...