Date of Award

12-1-2023

Degree Name

Master of Science

Department

Physics

First Advisor

Jayasekera, Thushari

Abstract

We computationally investigated the interaction between MHETase_BHET and MHETase_MHET complex using molecular dynamics simulation. MHET and BHET were placed in the active site of MHETase using molecular docking. We introduced mutation in the MHETase (R411K_F424I, R411K_F424V, R411K_F424N, R411K_S416A_F424I) structure to investigate the change in interaction profile. The complexes were equilibrated at 300k, and 2 ns molecular dynamics simulation was performed for every complexes. We used RMSD, SASA, RMSF, Radius of gyration, distance tools to analyze molecular dynamics trajectory. MD analysis revealed that mutated complex (R411K/S416A/F424I) shows highest activity toward BHET where wildtype MHETase does not show any activity toward BHET. In case of MHET, wild type MHET reflects the most favorable condition for interaction between MHETase and MHET. All other mutated complexes show less activity towards MHET than wild type.

Available for download on Tuesday, August 27, 2024

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