A role for confined water in chaperonin function |
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Authors: | England Jeremy L Lucent Del Pande Vijay S |
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Affiliation: | James H. Clark Center, S297, Stanford University, Stanford, California 94305, USA. |
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Abstract: | 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. |
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