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Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

Published on December 31, 2018   49 min

A selection of talks on Biochemistry

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0:00
Hello, I'm Jeff Kelly from the Scripps Research Institute and it's a privilege today to give a Henry Stewart talk. Focused on adapting the biology and/or chemistry of protein homeostasis to ameliorate diseases where protein aggregation causes degenerative phenotypes.
0:19
Even the most experienced scientists sometimes catch themselves thinking about translation as affording folded functional proteins.
0:30
But in fact, translation affords an unordered ensemble of conformers that generally speaking, have to fold in order to function, and while protein folding can be spontaneous. For the vast majority of human proteins, protein folding is assisted in some cases catalyzed by the protein homeostasis network. This is because of the reasons listed at the bottom of the slide in part. That is, there are chemical processes like peptidyl-prolyl amide bond isomerization and disulfide bond formation that are simply too slow to support life, and those processes must be catalyzed by enzymes.
1:14
Moreover, there's always a kinetic competition between protein folding, protein misfolding, and concentration dependent protein aggregation. And it's important that the biological components of the protein homeostasis network regulate these competitive processes such that sufficient function is maintained in the cell and in the extracellular space.

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Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

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