TL;DR: The results demonstrate that the folding rate of S-protein increases after the formation, or stabilization, of an intermediate which results from combination with S-peptide, and support a sequential model for protein folding in which the rates of successive steps in folding depend on the stabilities of preceding intermediates.

TL;DR: It appears that at least part of the H-bonded backbone of RNAase A is formed at an early stage in folding, since exclusion of water from the tertiary structure occurs later, as monitored by tyrosine absorbance.