[3]Kinetic mechanisms of protein folding
- 1 January 1986
- book chapter
- Published by Elsevier BV in Methods in enzymology
- Vol. 131, 51-70
- https://doi.org/10.1016/0076-6879(86)31034-6
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM(14–38)Journal of Molecular Biology, 1981
- Kinetic study of protein unfolding and refolding using urea gradient electrophoresisJournal of Molecular Biology, 1980
- Recombination of S-peptide with S-protein during folding of ribonuclease S: I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-proteinJournal of Molecular Biology, 1979
- Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease AJournal of Molecular Biology, 1978
- A folding model of α-lactalbumin deduced from the three-state denaturation mechanismJournal of Molecular Biology, 1977
- Kinetics of unfolding and refolding of proteins: III. Results for lysozymeJournal of Molecular Biology, 1973
- Kinetics of unfolding and refolding of proteins: I. Mathematical analysisJournal of Molecular Biology, 1973
- Kinetic evidence for intermediate states in the unfolding of chymotrypsinogen AJournal of Molecular Biology, 1972
- Folding of staphylococcal nuclease: Kinetic studies of two processes in acid renaturationJournal of Molecular Biology, 1971