The Stretch Molecular Dynamics Simulations Of The Interaction Between Hsp31and Its Substrate

Hsp31,as a molecular chaperone,plays an important role under stress conditionsby preventing the formation of protein aggregates and degrading misfolded proteins.This protein is normally seen in Escherichia Coli, which belongs to theDJ-1/ThiJ/Pfpl superfamily like DJ-1、YDR533Cp, etc. Apart from the proteinaseactivity known as we did, Hsp31also shows its glyoxalase activity toward glyoxaland methy glyoxal found in recent studies. In those studies, proteins in the Hsp31family are divided into three different classes on the basis of their superstructure. TheA domain and P domain are found simultaneously in class I; the class II catain an Adomain and an incompleted P domain; as for the class III proteins, there are just the Adomain found by us. In the active site of class I,there is an catalytictraid:Asp214-His186-Cys185which is much important for the proteinaseactivity.However, an alternative catalytic traid consisting of Cys185, His186and Glu77appears in class II and class III, which help the Hsp31catalytic the glyoxal.In order to learn more about those two activity of Hsp31,we have used thetheoretical method such as molecular docking, molecular dynamics simulation of allatoms and the stretching molecular dynamics simulation combined with thecalculation of the free energy on the basis of experimental data.