Protein/surface interactions are important in a variety of fields and devices, but fundamental understanding of the relevant phenomena is still in its infancy. Prevailing theories on the subject, which suggest that proteins should be stabilized when tethered to surfaces, do not explain the experimentally observed fact that proteins are often denatured on surfaces.  This presentation outlines simulation efforts to correlate protein stability on surfaces to structural features of the protein.  After describing the factors important in creating functional protein surfaces, results will be presented on how stability is correlated to the shape of the loop region in which the protein is tethered to the surface and the ability of the protein to vibrate on the surface. A detailed theory of protein stability on surfaces will then be presented. Finally, results will be shown on how surfaces can change the folding mechanism, by eliminating stabile intermediates, of proteins that fold through multistate mechanisms.  Taken as a whole the results offer hope that rational design of functional protein surfaces is possible once the behavior of the protein on the surface is ascertained. 

Predicting protein stabilities on surfaces

243rd National Meeting (2012)

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