Biophysical analysis reveals chaperonin folding efficiency correlates with cavity water affinity in bacterial GroEL, suggesting confined water directly shapes intracellular protein folding.
Chaperonins engulf other proteins and accelerate their folding by an unknown mechanism. Here, we combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin's ability to facilitate folding is correlated with the affinity of its interior surface for water. Our results suggest a novel view of the behavior of confined water for models of in vivo protein folding scenarios.
No takes yet. Share an insight, caveat, or question.
England et al. (2008) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: