THE EFFECTS OF COMBINING TWO DIFFERENT ALCOHOLS ON THE HEAT‐INDUCED REVERSIBLE DENATURATION OF RIBONUCLEASE
- 1 March 1974
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 6 (2) , 65-74
- https://doi.org/10.1111/j.1399-3011.1974.tb02362.x
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- THE EFFECT OF POLYHYDRIC AND MONOHYDRIC ALCOHOLS ON THE HEAT‐INDUCED REVERSIBLE DENATURATION OF LYSOZYME AND RIBONUCLEASEInternational Journal of Peptide and Protein Research, 1972
- Thermodynamics of protein denaturation. Effect of pressure on the denaturation on ribonuclease ABiochemistry, 1970
- Reversible Denaturation of Ribonuclease in Aqueous Solutions As Influenced by Polyhydric Alcohols and Some Other AdditivesJournal of Biological Chemistry, 1968
- Tertiary Structure of RibonucleaseNature, 1967
- Validity of the “two‐state” hypothesis for conformational transitions of proteinsBiopolymers, 1966
- The Effect of Aqueous Alcohol Solutions on the Thermal Transition of Ribonuclease1a,bThe Journal of Physical Chemistry, 1965
- Influence of water structure and of hydrophobic interactions on the strength of side‐chain hydrogen bonds in proteinsBiopolymers, 1963
- THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2The Journal of Physical Chemistry, 1962
- The Contribution of Hydrophobic Bonds to the Thermal Stability of Protein ConformationsJournal of Biological Chemistry, 1962
- Some Factors in the Interpretation of Protein DenaturationAdvances in Protein Chemistry, 1959