Science Advances

Supplementary Materials

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  • Supplementary Information Methods
  • fig. S1. The collapse dynamics of the extended polyubiquitin chain is slowed down upon DnaJ binding.
  • fig. S2. Specifically designed mutations in ubiquitin impair protein folding.
  • fig. S3. DnaJ blocks I27 refolding by binding to the collapsed (and not the native or extended) states.
  • fig. S4. Energetic cost of changing the dihedral angles upon DnaJ binding to the stretched ubiquitin.
  • fig. S5. Ramachandran plots for each ubiquitin fragment residue that interacts with DnaJ as a function of the pulling force.
  • fig. S6. The refolding kinetics of ubiquitin in the presence of DnaK cannot be captured by a single exponential.
  • fig. S7. The ATPase activity of DnaK is not increased upon incubation with ubiquitin.
  • fig. S8. DnaK recognizes the collapsed states of I27, blocking refolding.
  • fig. S9. Calculation of the binding (kon) and unbinding (koff) rate constants reveals that DnaJ and DnaK associate to different conformations of ubiquitin and I27.
  • fig. S10. Calculation of the binding (kextendedon) and unbinding (kextendedoff ) constants of DnaJ to the extended conformations of ubiquitin.
  • fig. S11. BSA does not affect the kinetics of ubiquitin refolding.
  • fig. S12. Independent addition of the different components of the KJE system improves the DnaK-mediated refolding of ubiquitin.
  • fig. S13. The complete DnaKJE system significantly enhances the rate and the extent of I27 refolding.
  • fig. S14. The DnaK system refolds the folding-inefficient titin (Z1)8 polyprotein.
  • fig. S15. Proposed sequences can be recognized by DnaK.
  • table S1. Summary of the kinetic parameters obtained after fitting for ubiquitin and I27.
  • Reference (49)

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