A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin
- 14 February 2000
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 84 (1) , 27-34
- https://doi.org/10.1016/s0301-4622(99)00140-4
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Energetics of structural domains in α‐lactalbuminProtein Science, 1996
- The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule stateNature Structural & Molecular Biology, 1994
- Energetics of the .alpha.-Lactalbumin States: A Calorimetric and Statistical Thermodynamic StudyBiochemistry, 1994
- Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study by differential scanning microcalorimetryJournal of Molecular Biology, 1992
- Thermodynamic parameters of β-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heatingThermochimica Acta, 1992
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Metal-Ion Binding and the Molecular Conformational Properties of α LactalbumiCritical Reviews in Biochemistry and Molecular Biology, 1989
- Stopped-flow kinetic studies of Ca(II) and Mg(II) dissociation in cod parvalbumin and bovine α-lactalbuminBiophysical Chemistry, 1987
- Influence of Ca2+ binding on the structure and stability of bovine α‐lactalbumin studied by circular dichroism and nuclear magnetic resonance spectraInternational Journal of Peptide and Protein Research, 1986
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981