Biophysical models of protein denaturation. I. An improvement of the model of two states
- 7 November 1991
- journal article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 153 (1) , 41-59
- https://doi.org/10.1016/s0022-5193(05)80352-2
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Common Features of Protein Unfolding and Dissolution of Hydrophobic CompoundsScience, 1990
- Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studiesBiochemistry, 1989
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988
- Protein stability curvesBiopolymers, 1987
- High-resolution differential scanning calorimetric analysis of the subunits of Escherichia coli aspartate transcarbamoylaseBiochemistry, 1985
- Thermodynamics of the binding of Streptomyces subtilisin inhibitor to .alpha.-chymotrypsinBiochemistry, 1985
- The thermodynamics of the self-association of the reduced and carboxymethylated form of apoA-II from the human high density lipoprotein complexBiochemistry, 1976
- Thermodynamic investigations of proteinsBiophysical Chemistry, 1976
- Calorimetric investigation of lysozyme thermal denaturationFEBS Letters, 1973
- The Thermodynamics of Protein Denaturation. I. The Denaturation of ChymotrypsinogenJournal of the American Chemical Society, 1964