Date of Award
2014
Document Type
Thesis
Degree Name
Bachelors
Department
Natural Sciences
First Advisor
Shipman, Steven
Keywords
Enzymes, Catalysis, B-lactamase, Chemistry
Area of Concentration
Chemistry
Abstract
Molecular dynamics have been carried out on b-lactamase CTX-M structures resolved by the Chen group at USF. Several protonation states of CTX-M were set up using the CHARMM simulation package in order to mimic the hydrolysis mechanism upon ligand binding. 11 ns simulations show a short intermolecular hydrogen bond between the catalytic triad Serine and Lysine in probable states. Aspartate residues outside of the active site also show evidence of an intermolecular short hydrogen bond, which may play a role in overall protein stability. These results support the proposed mechanism of ligand induced low barrier hydrogen bond formation by Cleland and Kreevoy. These results further validate the role of short intermolecular hydrogen bonds in protein catalysis.
Recommended Citation
Wang, Kenneth, "Enzymatic Catalysis in b-lactamases: Protonation States of the Catalytic Triad" (2014). Theses & ETDs. 4959.
https://digitalcommons.ncf.edu/theses_etds/4959