Multi-state transition for the thermal unfolding of certain globular proteins as evaluated from the analysis of DSC curve
- 1 June 1985
- journal article
- Published by Elsevier in Thermochimica Acta
- Vol. 88 (1) , 229-233
- https://doi.org/10.1016/0040-6031(85)85434-4
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Precision scanning calorimetry of bile salt-phosphatidylcholine micellesBiochemistry, 1982
- Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complexBiochemistry, 1981
- Thermodynamics of the binding of D-glucose to yeast hexokinaseBiochemistry, 1981
- Low Resolution Crystal Structures of Taka-Amylase A and Its Complexes with InhibitorsThe Journal of Biochemistry, 1979
- The lambda repressor contains two domains.Proceedings of the National Academy of Sciences, 1979
- Stability of Proteins Small Globular ProteinsAdvances in Protein Chemistry, 1979
- Papain denaturation is not a two‐state transitionFEBS Letters, 1978
- Precision scanning microcalorimeter for the study of liquidsThe Journal of Chemical Thermodynamics, 1975
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- ISOLATION OF CRYSTALLINE TAKA-AMYLASE A FROM “TAKADIASTASE SANKYO”The Journal of Biochemistry, 1954