Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

• DOI: 10.1126/science.271.5249.642
• Publication Date: 2006-10-27T18:30:41Z
• Authors: Ralph Zahn; Sarah Perrett; Gun Stenberg; Alan R. Fersht
• Keywords: Barnase; Bacillus amyloliquefaciens; Chaperone (clinical); Amide; Chaperonin; Folding (DSP implementation)

Hydrogen-deuterium exchange of 39 amide protons Bacillus amyloliquefaciens ribonuclease (barnase) was analyzed by two-dimensional nuclear magnetic resonance in the presence micromolar concentrations molecular chaperones GroEL and SecB. Both bound to native barnase under physiological conditions catalyzed deeply buried with solvent. Such required complete unfolding barnase, which occurred complex chaperones. Subsequent collapse unfolded exchange-protected folding intermediate markedly slowed or Thus, both have potential correct misfolding proteins annealing.