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At Johns Hopkins, Doug and his lab have been focusing on the folding of repeat proteins, and on the structure, energetics, and function of Notch signaling. The folding studies have involved a series of roughly translationally symmetric proteins that can be fragmented and extended, allowing direct correlations to be made between stability, folding kinetics, and protein structure. Using variable-length proteins made of identical “consensus”-based repeats, the Barrick lab has been able to apply nearest-neighbor “Ising” models to resolve intrinsic stability from coupling between repeats. This approach is providing a direct experimental quantification of cooperativity in protein folding, an important but difficult-to-characterize quantity.
These studies have also given rise to a more detailed study of consensus stabilization in globular proteins. The Barrick lab has recently had some surprising successes with this approach, and is currently extending and refining methods for consensus sequence design, to better understand why it works, why it sometimes fails, and how to make it work better. With these insights, we hope to be able to design high-value pharmaceutical and industrial proteins with improved stabilities, solubilities, and shelf-life.
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Journal of the American Chemical Societyno. 23 (2023): 12641-12650
Structure (London, England : 1993)no. 5 (2023): 584-594.e5
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