S. Walter Englander, University of Pennsylvania, "How do proteins do all of that as seen by hydrogen exchange. Protein folding, GroEL function, lipoprotein structure"
S. Walter Englander
Jacob Gershon-Cohen Professor of Medical Science
Professor of Biochemistry and Biophysics
University of Pennsylvania School of Medicine
Dr. Englander's laboratory is interested in biophysical studies of protein structure, function, folding, misfolding, and amyloid. Methods in use include the range of protein biophysical techniques including 2D NMR, chemical and spectroscopic approaches, analytical ultracentrifugation, electron microscopy, mass spectrometry, mutational analysis.
This laboratory has led in the development and use of hydrogen exchange (HX) approaches in protein and nucleic acid studies. HX measurements provide many dozens of probe points that are sensitive to structure, structure change, internal dynamics, energy, and functional interactions at identifiable positions throughout all macromolecules. The lab has developed and is using special hydrogen exchange methods that can measure the specific parts of any protein involved in any function, the protein folding process as it occurs on a sub-second time scale, the energetic stability of individual interactions, structure change, structure and dynamics in insoluble amyloids, etc.