The fundamental question that my group seeks to address is, how does a motor protein couple the energy from ATP binding and hydrolysis to perform mechanical work? To address this question we use chemical quenched-flow and fluorescence stopped-flow assays. Both techniques allow us to rapidly mix two reagents within 2 ms and observe a reaction on the millisecond time scale, which, in most cases, is the appropriate temporal resolution for enzyme catalysis.
To both design and interpret the rapid mixing kinetic experiments, one requires knowledge of the energetics of the binding and assembly reactions that occur. To address these questions, we use an array of thermodynamic, hydrodynamic, and spectroscopic approaches. These include analytical ultracentrifugation, dynamic and static light scattering, fluorescence titrations, and isothermal titration calorimetry (ITC), among others.
Just like physics seeks to describe phenomena with mathematics, biophysics seeks to describe molecular level events with mathematics. Thus, a major component of our work is using mathematics to quantitatively describe the observed physical phenomena. This is accomplished by using tools like Mathematica and Matlab to solve complex systems of both coupled differential and coupled algebraic equations. The derived solutions can then be used to model and describe the experimental results. This can often require coding in Matlab, C++, or Fortran.
In total, the research truly lies at the interface between Chemistry, Biology, Physics, and Mathematics. There is a place in my research group for members from each discipline.
Keywords - Physical Chemistry, Biophysical Chemistry, Thermodynamics of Protein-protein and Protein-ligand Interactions, Pre-steady State Kinetics, Enzyme Mechanism, and Motor Proteins
