Yale E. Goldman, MD, PhD

Professor

Lab Web Site

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615B Clinical Research Building

415 Curie Boulevard

Philadelphia, PA 19104

215-898-4017

Fax: 215-573-2653

goldmany@pennmedicine.upenn.edu

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Yale E. Goldman, MD, PhD


Professor of Physiology

Other Perelman School of Medicine Affiliations


Degrees & Education

  • BS, Northwestern University, 1968

  • MD, PhD, University of Pennsylvania, 1975


Awards & Honors

  • Upjohn Achievement Award, University of Pennsylvania

  • Trainee, Medical Scientist Training Program, University of Pennsylvania

  • Research Fellowship, Muscular Dystrophy Association

  • National Research Service Award, (NIH)

  • Research Career Development Award, (NIH)

  • Bowditch Lecturer of the American Physiological Society

  • Lindback Foundation Award for Distinguished Teaching

  • Lamport Lecturer of the University of Washington, School of Medicine

  • Distinguished Speaker for Graduate Student Research Forum, University of Cincinnati


Professional Affiliations

  • American Physiological Society

  • Society of General Physiologists

  • Physiological Society, U.K.

  • Physiological Society of Philadelphia Biophysical Society


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.


Key Words

  • Actin, Molecular motors, Motility, Myosin, Kinesin, Dynein, Structural dynamics, Fluorescence, Ribosome, Protein synthesis, G-Protein, Optical Trap, Single-Molecule, Nanotechnology


Research Description

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, bifunctional fluorescent probes and infrared optical traps (laser tweezers) to map the real-time domain motions of the motor proteins.

Protein Synthesis: Although the ribosome has been studied extensively since the unraveling of the genetic code, how it accomplishes the enormous fidelity of messenger RNA translation into amino acid sequences during protein biosynthesis is not understood. The ribosome is a motor translocating along the mRNA exactly 3 bases per elongation cycle. Energy from splitting GTP by G-protein elongation factors (EFs) is transformed into translational accuracy and maintenance of the reading frame. Codon-anticodon base pairing between mRNA and tRNA ‘reads’ the code, but EF-Tu ‘proofreads’ it. EF-G is the motor catalyzing translocation of tRNAs and mRNA. Powerful techniques developed for studies on motor proteins, including single molecule fluorescence and optical traps, may be applied to understand the structural biology, energetics, and function of EFs in their working environment./p>

Click here for a full list of publications.
(searches the National Library of Medicine's PubMed database.)


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