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Significance Protein confinement in compartments is ubiquitous in biology. Here, we show that a protein encapsulated in the GroEL/ES chaperonin cage is strongly destabilized owing, at least in part, to… Click to show full abstract
Significance Protein confinement in compartments is ubiquitous in biology. Here, we show that a protein encapsulated in the GroEL/ES chaperonin cage is strongly destabilized owing, at least in part, to a diminished hydrophobic effect. Hence, encapsulated protein substrates can undergo a process similar to cold denaturation in which the relatively ordered water in the cavity contributes to unfolding. Our results suggest that cavity-confined water can lead to protein unfolding in other biological compartments such as the proteasome.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
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