Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism

FEBS Letters

Miwa, S.²  Sugai, S.²  Yamaya, H.²  Kuwajima, K.²  Nagamura, T.¹ 

[1] Unisoku Inc., Ominemotomachi 1-28-5, Hirakata, Osaka 573-01, Japan;Department of Polymer Science, Faculty of Science, Hokkaido University, Kita-Ku, Sapporo, Hokkaido 060, Japan

关键词: Ferricytochrome c;    β-Lactoglobulin;    Protein folding;    Folding intermediate;    Stopped-flow;    Circular dichroism;    Cyt c;    cytochrome c;    βLG;    β-lactoglobulin;    GdnHCl;    guanidine hydrochloride;    N;    U;    native and unfolded states;   

DOI  :  10.1016/0014-5793(87)80363-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown