Event Information
Computational Insights into Functioning of Proteases and Design of their Synthetic Analogues
- Abstract:
The selective hydrolysis of the extremely stable peptide or amide bond of peptides and proteins is required in a wide range of biological, biotechnological and industrial applications such as control of the cell cycle, cell death, proteomics, protein engineering, designing of catalytic drugs and bioethanol production. We have applied innovative theoretical techniques including molecular dynamic (MD) simulations, quantum mechanics (QM) and quantum mechanics/molecular mechanics (QM/MM) to investigate the mechanisms of natural enzymes (aspartyl proteases and metalloproteases) and their synthetic analogues. The specific roles of metal ions, ligands and second coordination shell residues elucidated by these studies can be utilized to design more efficient synthetic analogues of peptide cleaving enzymes.
Host: David Beratan
Chemistry Seminar