Sedimentation equilibrium in reacting systems. VII. The temperature-dependent self-association of β-lactoglobulin A at pH 2.46
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference45 articles.
1. Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22
2. Molecular Interactions in β-Lactoglobulin. V. the Association of the Genetic Species of β-Lactoglobulin below the Isoelectric Point2
3. Molecular Interactions in β-Lactoglobulin. X. The Stoichiometry of the β-Lactoglobulin Mixed Tetramerization1
4. Molecular Interactions in β-Lactoglobulin. VI. the Dissociation of the Genetic Species of β-Lactoglobulin at Acid pH's2
5. Combined sedimentation and chemical equilibrium of β-lactoglobulin B in acid solution
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1. Approach to Study pH-Dependent Protein Association Using Constant-pH Molecular Dynamics: Application to the Dimerization of β-Lactoglobulin;Journal of Chemical Theory and Computation;2022-02-16
2. Bovine β-Lactoglobulin Is Dimeric Under Imitative Physiological Conditions: Dissociation Equilibrium and Rate Constants over the pH Range of 2.5–7.5;Biophysical Journal;2012-07
3. Effect of Temperature on the Self-Assembly of the Escherichia coli ClpA Molecular Chaperone;Biochemistry;2010-10-22
4. Protein self-association in solution: The bovine β -lactoglobulin dimer and octamer;Protein Science;2009-01-01
5. A High-Throughput Method for Detection of Protein Self-Association and Second Virial Coefficient Using Size-Exclusion Chromatography Through Simultaneous Measurement of Concentration and Scattered Light Intensity;Pharmaceutical Research;2007-06-19
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