Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation

@inproceedings{Geller2018Hsp90SP,
  title={Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation},
  author={Ron Geller and Sebastian Pechmann and Ashley Acevedo and Raul Andino and Judith Frydman},
  booktitle={Nature Communications},
  year={2018}
}
Acquisition of mutations is central to evolution; however, the detrimental effects of most mutations on protein folding and stability limit protein evolvability. Molecular chaperones, which suppress aggregation and facilitate polypeptide folding, may alleviate the effects of destabilizing mutations thus promoting sequence diversification. To illuminate how chaperones can influence protein evolution, we examined the effect of reduced activity of the chaperone Hsp90 on poliovirus evolution. We… CONTINUE READING
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