Steered molecular dynamic simulations of conformational lock of Cu, Zn-superoxide dismutase.

ABSTRACT: The conformational lock was a bio-thermodynamic theory to explain the characteristics of interfaces in oligomeric enzymes and their effects on catalytic activity. The previous studies on superoxide dismutases (Cu, Zn-SODs) showed that the dimeric structure contributed to the high catalytic efficiency and the stability. In this study, steered molecular dynamics simulations were used firstly to study the main interactions between two subunits of Cu, Zn-SODs. The decomposition process study showed that there were not only four pairs of hydrogen bonds but also twenty-five residue pairs participating hydrophobic interactions between A and B chains of SOD, and van der Waals interactions occupied a dominant position among these residue pairs. Moreover, the residue pairs of hydrogen bonds played a

SUBMITTER: Xiao BL 

PROVIDER: S-EPMC6416402 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature