Temperature‐dependence of the kinetics of folding of chymotrypsinogen A
- 15 June 1976
- journal article
- Published by Wiley in FEBS Letters
- Vol. 65 (3) , 293-296
- https://doi.org/10.1016/0014-5793(76)80132-9
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- Cooperative Conformational Changes in Globular ProteinsAngewandte Chemie International Edition in English, 1972
- Kinetic evidence for intermediate states in the unfolding of chymotrypsinogen AJournal of Molecular Biology, 1972
- Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximationBiochemistry, 1970
- On the kinetics of structural transition I of some pancreatic proteinsFEBS Letters, 1969
- Einfache Temperatursprung-Methode im Sekundenbis Stundenbereich und die reversible Denaturierung von ChymotrypsinEuropean Journal of Biochemistry, 1968