Role of proline isomerization in folding of ribonuclease A at low temperatures

AUTOR(ES)

Cook, Kem H.

RESUMO

In unfolded RNase A there is an interconversion between slow-folding and fast-folding forms (US ⇌ UF) that is known to show properties characteristic of proline isomerization in model peptides. Here, we accept the evidence that US molecules contain nonnative proline isomers and we ask about the isomerization of these proline residues during folding. The US ⇌ UF reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.

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