Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond.

Ítems similars

• Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor.
  per: Weissman, J S, et al.
  Publicat: (1992)
• The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.
  per: van Mierlo, C P, et al.
  Publicat: (1992)
• Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor.
  per: Staley, J. P., et al.
  Publicat: (1994)
• Genetic Selection for Enhanced Folding In Vivo Targets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor
  per: Foit, Linda, et al.
  Publicat: (2011)
• Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI)
  per: Buczek, Olga, et al.
  Publicat: (2002)