Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin
- 1 October 1971
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 10 (10) , 1865-1890
- https://doi.org/10.1002/bip.360101009
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Determination of stability of the DNA double helix in an aqueous mediumBiopolymers, 1969
- Method of determining the relative stability of different conformational states of biological macromoleculesBiopolymers, 1969
- Reversible thermal denaturation of Aplysia myoglobinJournal of Molecular Biology, 1968
- Thermodynamics of protein denaturation. III. Denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixturesJournal of the American Chemical Society, 1967
- Reversible Denaturation of Sperm Whale Myoglobin. I. Dependence on Temperature, pH, and CompositionJournal of the American Chemical Society, 1967
- Reversible Denaturation of Sperm Whale Myoglobin. II. Thermodynamic AnalysisJournal of the American Chemical Society, 1967
- Heat of Transition of Ribonuclease A1Journal of the American Chemical Society, 1965
- The Thermodynamics of Protein Denaturation. I. The Denaturation of ChymotrypsinogenJournal of the American Chemical Society, 1964
- Structural Studies of Ribonuclease. XI. Kinetics of DenaturationJournal of the American Chemical Society, 1963
- Myoglobin and the Structure of ProteinsScience, 1963