The Gulick Lab
Department of Structural Biology.
University at Buffalo.
Our work uses a variety of techniques to study protein structure and function;
The main goal of our work is to figure out how enzymes use specific structures to catalyze interesting chemical reactions. We use a variety of techniques, including molecular and structural biology, as well as enzymology and other biophysical tools to understand protein structure and function. We have additionally developed novel chemical inhibitors that can be used to probe protein function in biological systems.
In particular, we are focused on Natural Product Biosynthesis and the fascinating proteins that bacteria use to make novel chemicals. Our lab is interested in understanding the enzymatic basis for these biosynthetic pathways, as well as the role that novel compounds play in bacterial growth and pathogenesis.
While we are broadly interested in structure and function of a variety of enzymes, we have focused our attention on several enzyme families that are involved in natural product biosynthesis.
A family of adenylate forming enzymes that include acyl-CoA synthetases, NRPS adenylation domains, and beetle luciferase enzymes.
NRPS enzymes are large, modular assembly line proteins that produce important peptides, including antibiotics and siderophores.
Many bacteria produce hydroxamate siderophores for iron acquisition, using a family of ligases that catalyze amide linkages.
Andrew M. Gulick
Professor,
Department of Structural Biology
Jacobs School of Medicine and Biomedical Sciences
University at Buffalo
955 Main St.
Buffalo, NY 14203-1121
PH (716)829-3696
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School of Medicine Faculty Page
Admission to our graduate program occurs through the PPBS, an interdisciplinary PhD Program in Biological Sciences at UB.