Article
Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation.
Nature communications - 3 May 2018
Geller Ron, Pechmann Sebastian, Acevedo Ashley, Andino Raul, Frydman Judith
Abstract excerpt
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...
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