Cooperativity in the unfolding transitions of cysteine proteinases. Calorimetric study of the heat denaturation of chymopapain and papain
- 1 November 1993
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1203 (1) , 121-125
- https://doi.org/10.1016/0167-4838(93)90045-s
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Thermodynamics of Structural Stability and Cooperative Folding Behavior in ProteinsPublished by Elsevier ,1992
- A simple model for proteins with interacting domains. Applications to scanning calorimetry dataBiochemistry, 1989
- Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Biochemical Applications of Differential Scanning CalorimetryAnnual Review of Physical Chemistry, 1987
- Structure of papain refined at 1.65 Å resolutionJournal of Molecular Biology, 1984
- Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein FoldingAnnual Review of Biochemistry, 1982
- Stability of ProteinsPublished by Elsevier ,1982
- Stability of Proteins Small Globular ProteinsAdvances in Protein Chemistry, 1979
- Papain denaturation is not a two‐state transitionFEBS Letters, 1978
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974