The Thermal Stability of Immunoglobulin: Unfolding and Aggregation of a Multi-Domain Protein
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- 31 January 2000
- journal article
- Published by Elsevier
- Vol. 78 (1) , 394-404
- https://doi.org/10.1016/s0006-3495(00)76602-1
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH‐induced stateFEBS Letters, 1995
- Comparative thermodynamic analyses of the Fv, Fab* and Fab and Fab fragments of anti-dansyl mouse monoclonal antibodyFEBS Letters, 1995
- Cooperativity in the unfolding transitions of cysteine proteinases. Calorimetric study of the heat denaturation of chymopapain and papainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- DSC studies on the denaturation and aggregation of serum albuminsThermochimica Acta, 1992
- Proteins in aqueous solutions. calorimetric studies and thermodynamic characterizationThermochimica Acta, 1991
- Domain association in immunoglobulin moleculesJournal of Molecular Biology, 1985
- Multi-state transition for the thermal unfolding of certain globular proteins as evaluated from the analysis of DSC curveThermochimica Acta, 1985
- Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chainJournal of Molecular Biology, 1982
- Comparative study of the conformational features of rat immunoglobulin G subclasses by circular dichroismBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980