A role for confined water in chaperonin function.
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.
England
Jeremy L
JL
James H. Clark Center, S297, Stanford University, Stanford, California 94305, USA.
Lucent
Del
D
Pande
Vijay S
VS
D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D017510:Protein Folding; D014867:Water / Q000737:chemistry* / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D014867:Water; D018833:Chaperonins