Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism
Open Access
- 31 August 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 221 (1) , 115-118
- https://doi.org/10.1016/0014-5793(87)80363-0
Abstract
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.Keywords
This publication has 12 references indexed in Scilit:
- Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozymeBiochemistry, 1986
- The structure of β-lactoglobulin and its similarity to plasma retinol-binding proteinNature, 1986
- Dynamics of the disordered–β transition in poly(L‐tyrosine) determined by stopped‐flow spectrometryBiopolymers, 1986
- Stopped-flow X-ray scatterign device with a slit-type mixerJournal of Biochemical and Biophysical Methods, 1985
- ‘Molten‐globule“ state accumulates in carbonic anhydrase foldingFEBS Letters, 1984
- Protein FoldingAnnual Review of Biochemistry, 1981
- Nature of the fast and slow refolding reactions of iron(III) cytochrome cBiochemistry, 1981
- Kinetics of the helix—coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurementsBiophysical Chemistry, 1978
- Beta poly(l-lysine): A model system for biological self-assemblyJournal of Molecular Biology, 1974
- Simple procedures for the separation and identification of bovine milk whey proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973