作者: S��lvia Bronsoms , Josep Villanueva , Francesc Canals , Enrique Querol , Francesc X. Aviles
DOI: 10.1046/J.1432-1033.2003.03754.X
关键词:
摘要: Protein folding can be modulated in vivo by many factors. While chaperones act as catalysts and show broad substrate specificity, some pro-peptides specifically facilitate the of mature protein to which they are bound. Potato carboxypeptidase inhibitor (PCI), a 39-residue inhibitor, is synthesized precursor that includes 27-residue N-terminal seven-residue C-terminal pro-regions. In this work disulfide-coupled PCI vitro has been compared with same extended either pro-sequence (ProNtPCI) or both N- pro-sequences (ProPCI), also trans (ProNt + PCI). No significant differences observed kinetics efficiencies all these molecules. addition, studies Escherichia coli have performed using wild-type three mutant forms without pro-sequence, mutations had previously reported affect form. The extent 'native-like' form was secreted media each construction not affected presence pro-sequence. These results indicate does depend on for its both, E. coli. However, structural analysis spectroscopy, hydrogen exchange limited proteolysis mass spectrometry, capability such fold within