@article{oai:ir.soken.ac.jp:00004137,
 author = {桑島, 邦博 and KUWAJIMA, Kunihiro and YAMAYA, Hidetoshi and MIWA, Soichi and SUGAI, Shintaro and NAGAMURA, Thoshihiko},
 issue = {1},
 journal = {FEBS Letters, FEBS Letters},
 month = {Aug},
 note = {Kinetic refolding reactions of ferricytochrome c and β-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.},
 pages = {115--118},
 title = {Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism},
 volume = {221},
 year = {1987}
}