Numerical study of the effect of thiol–disulfide exchange in the cluster phase of β-lactoglobulin aggregation
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2012/FD/C2FD20030A
Reference28 articles.
1. Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
2. Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings
3. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150°C. a review
4. β-Lactoglobulin and WPI aggregates: Formation, structure and applications
5. Heat-Induced Aggregation of β-Lactoglobulin: Role of the Free Thiol Group and Disulfide Bonds
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1. Toward Automated Sampling of Polymorph Nucleation and Free Energies with the SGOOP and Metadynamics;The Journal of Physical Chemistry B;2021-11-17
2. Fractal Dimension Analysis of Texture Formation of Whey Protein-Based Foods;International Journal of Food Science;2018
3. Moving from molecules, to structure, to texture perception;Food Hydrocolloids;2017-07
4. Exposure of thiol groups in the heat-induced denaturation of β-lactoglobulin;Molecular Simulation;2014-07-07
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