Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism.
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.
D002942:Circular Dichroism; D003574:Cytochrome c Group; D007700:Kinetics; D007782:Lactoglobulins; D011487:Protein Conformation
D003574:Cytochrome c Group; D007782:Lactoglobulins