Trans-Disiplinary Research.


    Utilizing the foundation of protein and biochemical techniques, introducing a multitude of medical applications and research innovation.

    Biophysical Science.

    Combining the sciences to study the motional dynamics of intrinsically disordered protein stathmin by SDSL-EPR.

    Physical Chemistry.

    Techniques used in quantifying motion at the molecular level, creating a potential for analyzing Microsystems.

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About the Lab.

Dr. Michael Bridges' research is centered on studying the intrinsic motion of the protein stathmin. One objective is to identify the physical attributes of the folded states using various physical and biochemical techniques.

  • Discovering the physical dynamics of the intrinsic protein Stathmin upon binding to Tubulin protein.
  • Using Site Directed Mutagenesis Technique to attatch a Nitroxide label to the Stathmin Protein
  • Using EPR technology to display radical activity on the spin labeled Stathmin protein

Research Interests

Dr. Bridges' general research focus is centered on the study of small, intrinsically unstructured proteins and the changes to their motional dynamics upon binding, activation, phosphorylation, etc. Of particular interest is the cytoskeletal regulation protein, stathmin (or oncoprotein-18) - the configurational and dynamical changes it undergoes upon binding to microtubules and free tubulin. The goal is to elucidate the mechanism of microtubule destabilization by Stathmin as a function of phosphorylation level, employing the techniques of side-directed mutagenesis, nitroxide spin labeling of free protein cysteines, and electron paramagnetic resonance (EPR) spectroscopy.

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