How do proteins do all of that as seen by hydrogen exchange. Protein folding, GroEL function, lipoprotein structure

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Author(s)
Englander, S. Walter
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School of Biological Sciences
School established in 2016 with the merger of the Schools of Applied Physiology and Biology
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http://hdl.handle.net/1853/39024
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.
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Date
2011-05-10
Extent
63:21 minutes
Resource Type
Moving Image
Resource Subtype
Lecture
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