Forced Unfolding of Mesophilic Cold Shock Protein Studied by Steered Molecular Dynamics Simulation
嗜温冷休克蛋白力致去折叠研究

Mesophilic cold shock protein possesses a five-stranded antiparallel β-barrel, which was investigated experiment of unfolded recently. Molecular dynamics simulation has been used to investigate the force-induced unfolding of mesophilic cold shock protein, finding that the unfolding process occur through intermidate states. Both constant velocity and constant force stretching have been employed to model forced unfolding of Mesophilic Cold Shock Protein, the result that unfolding process of the protein complied with the same sequesce in these two method was obtained, namely unfolding of C-terminal strands at first, subsequently unfolding of N-terminal, and the two methods all showed clear evidence of intermediate states. The results of SMD simulations elucidate that mesophilic cold shock protein is protected against external stress mainly through the interstrand hydrogen bonding, and the ions pair also play an important role in the process of unfolding.