Kuwajima K, Yamaya H, Miwa S, Sugai S, Nagamura T
FEBS Lett. 1987 Aug 31;221(1):115-8. doi: 10.1016/0014-5793(87)80363-0.
Kinetic refolding reactions of ferricytochrome c and beta-lactoglobulin have been studied by stopped-flow circular dichroism by monitoring rapid ellipticity changes of peptide backbone and side-chain chromophores. In both proteins, a transient intermediate accumulates within the dead time of stopped-flow mixing (18 ms), and the intermediate has an appreciable amount of secondary structure but possesses an unfolded tertiary structure. It is suggested that the rapid formation of a secondary structure framework in protein folding is a common property observed in a variety of globular proteins.
