Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
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Updated: Oct 21, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Abstract:
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.
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