Yale Goldman, M.D., Ph.D., is Professor of Physiology at the University of Pennsylvania. He is also faculty in the Biochemistry & Molecular Biophysics and Cell & Molecular Biology graduate groups.
Dr. Goldman’s research seeks to relate 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.
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. The Goldman research group is using novel biophysical techniques, including nanometer tracking of single fluorescent molecules, bifunctional fluorescent probes and infrared optical traps (laser tweezers) to map the real-time domain motions of the motor proteins.
Keywords: mapping domain motions of motor proteins and ribosomal elongation factors; mechanics of the energy transduction mechanism; enzymatic reactions; myosin; dynein; kinesin; nanometer tracking of single fluorescent molecules and fluorescent probes; optical traps; mechanobiology
Working Group(s): Working Group 1: How do cells sense their mechanical environment?; Working Group 3: How do cells remember their mechanical environment?; Working Group 4: Crosscutting and Emerging Technologies