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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.
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