Publications by authors named "Corey R Siegel"
Article Synopsis
- RNase A folds more quickly with disulfide bonds intact compared to when it undergoes oxidative folding from a reduced state.
- Researchers studied mutants Y92G, Y92A, and Y92L to understand how native interactions impact both conformational and oxidative folding pathways of the protein.
- Although the overall folding pathway remained unchanged, Y92G and Y92A mutants destabilized a key disulfide-bonded species in the oxidative folding pathway, highlighting the protective role of specific interactions during protein folding.
