S. Walter Englander, University of Pennsylvania, "How do proteins do all of that as seen by hydrogen exchange. Protein folding, GroEL function, lipoprotein structure"

May 10 2011, 11:00 am
Distinguished Lecture Series Guest Speaker: 

S. Walter Englander

Jacob Gershon-Cohen Professor of Medical Science
Professor of Biochemistry and Biophysics
University of Pennsylvania School of Medicine

Date & Time: 
Tuesday, May 10, 2011, 11:00AM
Location: 
Klaus 1116E
Host: 
Jeffrey Skolnick
Abstract: 
The talk will illustrate the use of hydrogen exchange methods to learn about biophysical properties and functional behaviors of protein molecules. Hydrogen exchange has been measured by older tritium exchange techniques, by 2D NMR, and most recently by mass spectrometry. Examples of applications will illustrate how each method provides specific advantages for different applications. Topics to be considered include how proteins fold, and how GroEL helps proteins to fold. Also recent progress in extending hydrogen exchange to the study of large and even insoluble protein systems using mass spectrometry will be shown.
Additional Info: 

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.

Faculty Website
Lab Website
Walter Englander - Seminar Flier.jpg

Video: 
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