Genomic sequencing has led to a wealth of newly discovered protein sequences. However, the functions of the majority of these proteins remain experimentally untested. Sequence databases are filled with functional annotations that are guesses based on sequence similarity to characterized proteins. Unfortunately, the residues that regulate binding specificity and catalysis represent only a small subset of the overall protein architecture. Subsequently, sequence alignments often fail to distinguish between proteins with similar sequences but divergent functions, or fail to recognize proteins that display low sequence similarity but share similar folds and functions.
My research involves the design and implementation of high-throughput enzyme activity assays. This work is being done in conjunction with the Center for Eukaryotic Structural Genomics, which maintains a high-throughput protein production facility as part of their mandate to solve novel structures and develop methods for improving protein production efficiency.