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The relationship between protein structure and function
Work in our lab uses X-ray crystallography and functional biochemistry to determine how enzymes function at a molecular level. A complete understanding of the ways that enzymes are able to catalyze chemical reactions is both interesting and raises the possibility of designing new enzymes to perform additional chemical reactions. Our work provides atomic resolution details concerning the role of specific residues in an enzyme active site, "What role does the side chain of Arg584 play in binding substrate?" or "Why is Trp32 universally conserved in all related proteins?"
Additionally, the genome sequencing projects have identified the genes, and therefore the proteins, present in many organisms. While many proteins have known functions, nearly half of the proteins encoded in bacterial and eukaryotic genomes are annotated as "protein of unknown function". Studying proteins both structurally, with X-ray crystallography, and functionally, with any of a number of biochemical, molecular, and biological techniques, can provide insights into the relation of enzyme structure and function may prove useful in identifying the function of these uncharacterized proteins.
The proteins that we are studying are primarily bacterial proteins that either show novel biochemical properties, making them interesting examples of the how enzymes have evolved to function efficiently, or are essential proteins that may be targets for antibiotic development. An inhibitor that blocks a step that is essential for bacterial growth or virulence may be a lead compound for a novel antibiotic.
