Mechanical Rigidity of DNA and its Relation to DNA-Protein Interactions

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Dr. Austin is studying the sequence dependence of the elastic properties of DNA and its implications for specificity in protein-DNA interactions. The goals are ambitious and involve the complete integration of physical and biological methodology. Until recently crystallographic data were only available for isolated protein or DNA molecules, that is, not docked together in a biological complex. As a result, models for site specific protein binding have often had a "lock and key" quality. They attempt to understand recognition in terms of a simple interaction between rigid and non--allosteric partners. This project will attempt to show that the bending and torsional strain stored in DNA upon complexation is of equal importance in binding specificity.