Michael Trakselis Assistant Professor, Chemistry


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Pittsburgh, PA


Mechanism and Design of Molecular Machines

Keywords: rotaxanes, processive catalysis, proteins, enzymes, macromolecular interactions

We aim to understand how processive enzymes interact with and translocate along DNA to perform various functions in DNA replication and repair. These molecular machines including: Trakselis 1DNA helicases, polymerases, and clamps, are remarkable in their enzymatic efficiency and have evolved with high specificities towards their substrate. In order to obtain the processivity and specificity, these enzymes have evolved a common toroidal or circular architecture to remain tightly associated with their templates. At the same time, we aim to take advantage of this evolved architecture to engineer biohybrid protein catalysts to act along nontraditional template. For example, circular proteins are being designed to act as molecular switches that respond reversibly to changes in solutions conditions and light. Processive biohybrid catalysts that incorporate the best aspects from chemistry and biology are also being deigned to react along natural DNA and unnatural polymeric templates. Research in our laboratory is extremely multidisciplinary and designed to reveal unknown mechanisms of protein molecular machines for inspiration in engineering novel properties and reactions at the nanoscale level.


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