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| Name |
Goldman, Yale E. |
| Location
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University of Pennsylvania School of Medicine |
| Primary Field
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Biophysics and Computational Biology |
| Secondary Field
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Physiology and Pharmacology |
 Election Citation
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Goldman has exploited a spectacular array of biophysical techniques, including the latest generation of single-molecule approaches, to determine how ATP hydrolysis is coupled to biochemical and conformational changes in motor proteins that power force generation and work. He is a tireless advocate for application of nanotechnology to physiological problems. |
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Research Interests
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My laboratory studies cell motility and protein synthesis. 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 power many cell biological motions such as targeted vesicle transport and cell division. The ribosome translates codons in messenger RNAs into amino acid sequences with enormous speed and fidelity. Energy from splitting GTP by G-protein elongation factors (EFs) is transformed into translational accuracy and maintenance of the reading frame. We relate the structural changes in these macromolecules to the chemical and mechanical steps of the energy transduction mechanism by mapping the real-time domain motions and kinetics of the motor proteins and ribosomal elongation factors. We have developed and apply novel biophysical methods including laser photolysis of caged substrates, for instance caged ATP, nanometer tracking of position and orientation of single fluorescent probes and ultra-fast feedback infrared optical traps. The biophysical mechanisms of stepping along these machines' tracks, how they are optimized for their various specific roles in the cell, and how they work together in teams are some of the outstanding research questions and areas of progress. |
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