Anfinsen Redux: Ribonuclease Folding in the Single-Molecule Regime

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Single-molecule enzymology reveals distinct renaturation pathways in ribonuclease A, suggesting hidden details in its folding kinetics.

Fast and slow refolding kinetics were observed in individual ribonuclease A molecules, indicating molecular heterogeneity.
The study highlights the role of slow prolyl peptide bond isomerization in the distinct renaturation pathways of RNase A.
Single-molecule enzymology was used to monitor catalytic recovery in urea-denatured ribonuclease A at the molecular level.
These findings underscore the advantages of single-molecule techniques in uncovering complexities of protein folding.

Melkonian et al. (2025) studied this question.

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