Background:The enzyme DsbA is essential for production of disulfide-bonded proteins in E. coli. Results: The folding, misfolding, and release kinetics of a substrate interacting with DsbA are determined from single molecule observations. Conclusion: DsbA is much more effective than its eukaryotic counterpart. Significance: Previous mechanistic models are generalized while providing insight into the kinetic parameters that influence oxidative folding outcomes.

Background: Lou Gehrig's disease is accompanied by misfolding and aggregation of proteins. Results: The intramolecular reactivity of cysteines of superoxide dismutase 1 results in new disulfide bonds in unusual positions. Conclusion: Thiol/disulfide exchange reactions are altered in mutated proteins. Significance: Intramolecular reorganization of disulfides may be one of the mechanisms of protein misfolding related to neurodegenerative diseases.

No abstract

No abstract