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Structural prediction, design and folding of integral membrane proteins

We are interested in understanding the folding and structural properties of integral membrane proteins, and how these properties ultimately relate to their function.

Membrane proteins fold in a complex environment, following rules that are different from those that apply to soluble proteins. However, these rules are still less understood because of the difficulties encountered in the expression, purification and biophysical characterization of this very hydrophobic class of proteins.

To obtain much need structural and biophysical information, our laboratory adopts a multidisciplinary approach, using and developing an integration of computational and experimental methods to reach beyond the limits of individual techniques.

We take advantage of the growing structural and genomic databases, using statistical analysis to identify motifs that are important for the folding and function of membrane proteins.

We measure their folding and association in the laboratory and develop structural prediction methods that can incorporate the experimental constraints obtained from "low resolution" methods such as mutagenesis or crosslinking.

Finally, we use protein design to test and validate our current understanding of the principles that govern structure and folding in the membrane, and to create novel proteins with a desired function.