Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A
- 25 January 1978
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 118 (3), 317-330
- https://doi.org/10.1016/0022-2836(78)90231-0
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolinePeptide Science, 1977
- A quantitative treatment of the kinetics of the folding transition of ribonuclease ABiochemistry, 1976
- A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groupsJournal of Molecular Biology, 1975
- The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding speciesJournal of Molecular Biology, 1975
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- Kinetics of unfolding and refolding of proteins: II. Results for cytochrome cJournal of Molecular Biology, 1973
- Validity of the “two‐state” hypothesis for conformational transitions of proteinsPeptide Science, 1966
- The Thermodynamics of Protein Denaturation. II. A Model of Reversible Denaturation and Interpretations Regarding the Stability of ChymotrypsinogenJournal of the American Chemical Society, 1964
- The Thermodynamics of Protein Denaturation. I. The Denaturation of ChymotrypsinogenJournal of the American Chemical Society, 1964
- The Configurational Changes of Poly-L-proline in SolutionJournal of the American Chemical Society, 1960