Real-time and equilibrium (19)F-NMR studies reveal the role of domain–domain interactions in the folding of the chaperone PapD

Lignende værker

• PapD-like chaperones provide the missing information for folding of pilin proteins
  af: Barnhart, Michelle M., et al.
  Udgivet: (2000)
• Catalysis of protein folding by chaperones in pathogenic bacteria
  af: Bann, James G., et al.
  Udgivet: (2004)
• Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.
  af: Slonim, L N, et al.
  Udgivet: (1992)
• PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.
  af: Jacob-Dubuisson, F, et al.
  Udgivet: (1994)
• FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.
  af: Jones, C H, et al.
  Udgivet: (1993)