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Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism 桑島, 邦博 KUWAJIMA, Kunihiro YAMAYA, Hidetoshi MIWA, Soichi SUGAI, Shintaro NAGAMURA, Thoshihiko metadata only access © 1987 Published by Elsevier B.V. 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. Elsevier 1987-08-31 eng journal article https://ir.soken.ac.jp/records/4137 3040467 https://doi.org/10.1016/0014-5793(87)80363-0 10.1016/0014-5793(87)80363-0 0014-5793 FEBS Letters FEBS Letters 221 1 115 118