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Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism
Author(s) -
Kuwajima K.,
Yamaya H.,
Miwa S.,
Sugai S.,
Nagamura T.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80363-0
Subject(s) - circular dichroism , chemistry , protein secondary structure , folding (dsp implementation) , chromophore , stopped flow , protein folding , globular protein , protein tertiary structure , crystallography , biophysics , protein structure , side chain , kinetics , photochemistry , biochemistry , organic chemistry , reaction rate constant , polymer , physics , quantum mechanics , electrical engineering , biology , engineering
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.