My main research interest is the structure-function relationship in membrane proteins and its application to drug discovery. Membrane proteins mediate the cell exchange of energy, nutrients and information. They are highly relevant to human physiology and disease (eg. depression, diabetes, multidrug resistance). Rational drug design relies on understanding the molecular basis of a protein’s function. Nevertheless, determination of the three-dimensional structure of membrane proteins continues to be an arduous task; less than 1% of their structures are known. I am particularly interested in secondary transport proteins, members of one of the largest membrane proteins superfamily, the Major Facilitator Superfamily (MFS). The structural technique of choice for MFS proteins is x-ray protein crystallography. In our laboratory, we apply high-throughput methodologies for protein expression and crystallization. Besides x-ray protein crystallography, we routinely use membrane protein biochemistry, molecular biology and structural modeling.
