We are studying the relationship between structure and function in three different types of proteins: 1) antifreeze proteins (AFPs), which help organisms resist or tolerate freezing; 2) bacterial adhesins, which help their bacterial hosts bind and colonize specific surfaces; and 3) calpains, enzymes that selectively cut proteins within the cell in response to calcium signaling.

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Included in our research on antifreeze proteins is the study of bacterial ice nucleation proteins, which cause frost damage to plants. Although they have the opposite function to antifreeze proteins – starting ice growth, rather than stopping it – there is evidence to suggest they both use a similar mechanism of action in organizing ice-like waters on the protein surface.

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Our research projects involve bioinformatics, gene synthesis and cloning, the production and purification of natural and recombinant proteins, biophysical and structural analyses, cellular analyses, protein modeling and protein engineering.