Albany 2019: 20th Conversation - Abstracts

category image Albany 2019
Conversation 20
June 11-15 2019
Adenine Press (2019)

Protein Folding Energetics and Proteostasis: A Two-Way Connection

Proteostasis is the condition of a cell or organism having enough natively folded protein to carry out essential biological functions while suppressing protein misfolding and aggregation to levels below those that would cause toxicity. Protein folding to the native state can occur spontaneously, but often does not, with protein instead becoming trapped in non-functional misfolded or aggregated states. Because of this, all organisms have a proteostasis network: a collection of chaperones and proteases that shepherd protein to the native state or recover or dispose of protein that has misfolded or aggregated. We have used computational models of in vivo protein folding in the presence of the proteostasis network to deepen our understanding of how organisms maintain proteostasis. Here we will describe the insights that these models have provided into how protein folding energetics read through to proteostasis and also how these models can, in a sense, be inverted, to use perturbations in proteostasis to learn about protein folding energetics.
This research has been supported by the NIH (grant GM101644).

Evan T. Powers

Department of Chemistry
Scripps Research
La Jolla, CA 92037

Ph: (858) 784-9609
Email: epowers@scripps.edu