NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms

Analyses of locations and structural distortions following the removal of the Cys65-Cys72 disulfide bond were done as a means of determining the structural differences between the three-dimensional folding intermediate and the wt RNase A. Removal of disulfide bonds results in an increase in 1H/2H exchange rates for backbone amides located throughout the 'protein fold.