The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding species
- 5 June 1975
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 94 (4) , 611-620
- https://doi.org/10.1016/0022-2836(75)90325-3
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Kinetics of refolding of guanidine hydrochloride denatured cytochrome c. Temperature dependenceBiochemistry, 1973
- Kinetics of unfolding and refolding of proteins: I. Mathematical analysisJournal of Molecular Biology, 1973
- Kinetics of unfolding and refolding of proteinsJournal of Molecular Biology, 1973
- Inactivation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic determinantBiochemistry, 1972
- Simple sequential model for the kinetics of conformational transitions of oligomeric helices and proteinsBiopolymers, 1972
- Kinetics of conformation change of sperm-whale myoglobin. I. Folding and unfolding of metmyoglobin following pH jumpBiochemistry, 1972
- Folding of staphylococcal nuclease: Kinetic studies of two processes in acid renaturationJournal of Molecular Biology, 1971
- Kinetic Evidence for Incorrectly Folded Intermediate States in the Refolding of Denatured ProteinsNature, 1971
- The denatured states of ribonucleaseJournal of Molecular Biology, 1964
- Structural Studies of Ribonuclease. V. Reversible Change of Configuration1-3Journal of the American Chemical Society, 1961