Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways.

Abstract excerpt

Evidence that proteins may unfold utilizing complex competing pathways comes from a new pulse-labeling protocol in which the change in reactivity of a single cysteine residue in a protein during unfolding is measured, making use of its easily monitored reaction with the Ellman reagent, dithionitrobenzoic acid. The kinetics of unfolding of two single cysteine-containing mutant forms of the small protein barstar,...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Binding, Competitive
• Share to Cysteine
• Share to Fluorescence