Thermodynamic parameters for 3-state thermal denaturation of human and bovine α-lactalbumin
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,Condensed Matter Physics,Instrumentation
Reference25 articles.
1. Lysozyme and α-Lactalbumin: Structure, Function, and Interrelationships
2. Metal-Ion Binding and the Molecular Conformational Properties of α Lactalbumi
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4. Phylogenetic Variations in the Calcium-Dependent Electrophoretic Shift of α-Lactalbumin
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1. Polyethylene glycol induced structural modulation of holo alpha-lactalbumin: In vitro and in vivo approach towards protein stability;Journal of Molecular Liquids;2023-07
2. Influence of thermomechanical treatment and pH on the denaturation kinetics of highly concentrated whey protein isolate;Journal of Food Engineering;2021-03
3. Influence of Thermomechanical Treatment and Ratio of β-Lactoglobulin and α-Lactalbumin on the Denaturation and Aggregation of Highly Concentrated Whey Protein Systems;Foods;2020-08-29
4. Structure and Stability Analysis of Cytotoxic Complex of Camel α-Lactalbumin and Unsaturated Fatty Acids Produced at High Temperature;Journal of Biomolecular Structure and Dynamics;2011-06
5. Influence of calcium on the thermal stabilization of bovine α-lactalbumin by selected polyols;Journal of Thermal Analysis and Calorimetry;2010-12-16
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