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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Deciphering Substrate Promiscuity By Aminoglycoside Resistance Enzymes Via A Biophysical Characterization And Dynamics Of The Aminoglycoside Acetyltransferase-(3)-Iiib And The Aminoglycoside Phosphotransferase-(3′)-Iiia, Adrianne Lee Norris
Doctoral Dissertations
Aminoglycoside antibiotics are losing their bactericidal efficacy due to the spread of enzymes that catalyze a covalent modification to them. A common property of many of these aminoglycoside modifying enzymes (AGMEs) is the capacity to modify multiple diverse aminoglycosides thus conferring resistance to these drugs among several pathogenic bacterial species. To gain a better understanding of the protein-antibiotic interactions responsible for resistance and the promiscuous nature of AGMEs, a variety of biophysical techniques including nuclear magnetic resonance (NMR), isothermal titration calorimetry (ITC), steady state kinetics, intrinsic tryptophan fluorescence, and computational modeling are employed in this work. Results and discussion presented …
Understanding The Thermodynamics Of Enzyme-Antibiotic Interactions With Aminoglycoside Phosphotransferase-3’-Iiia, Michele K. Miller
Understanding The Thermodynamics Of Enzyme-Antibiotic Interactions With Aminoglycoside Phosphotransferase-3’-Iiia, Michele K. Miller
Chancellor’s Honors Program Projects
No abstract provided.