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Prism type TIRF used in polarized fluorescence experiments.
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Microscope stage used for optical trapping and TIRF experiments.
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Redirected laser used for polarized fluorescence experiments.
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Several of the lasers and electronics used for optical trapping and TIRF experiments.
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Four color capability for FRET experiments.
Yale E. Goldman Lab
Research Interests
Relating the structural changes to enzymatic reactions and mechanical steps of the energy transduction mechanism by mapping the real-time domain motions of the motor proteins and ribosomal elongation factors.
Keep on Truckin'!
Molecular Motors
Motor proteins and GTP-binding proteins (G-proteins) share many structural and functional attributes. Molecular motors myosin, dynein and kinesin are prototype biological energy transducers that can be understood at a particularly fine level of detail. The obvious functional output (force and motion) allow the reaction sequence to be probed by single molecule biophysical, chemical and structural studies. A cyclic interaction between actin and myosin transforms free energy of splitting ATP into motion and mechanical work. Modified forms of this mechanism power other cell biological motions such as targeted vesicle transport and cell division. We are using novel biophysical techniques, including nanometer tracking of single fluorescent molecules, FRET sensors, bifunctional fluorescent probes and infrared optical traps (laser tweezers) to map the real-time domain motions of the motor proteins.