Molecular simulation of partially denatured β-lactoglobulin
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Le résumé fourni par la source
The unfolding of β-lactoglobulin (β-lac) upon heating was comprehensively studied through molecular dynamics computer simulations. A β-lac molecule in the aqueous solution was firstly heated at 500 K for unfolding and then annealed at 300 K to collect stable conformations. There were five meta-stable conformations observed based on the Free Energy Landscape (FEL). The β-lac molecule was found to exhibit an open and extended conformation on heating followed by limited refolding upon cooling. The cysteine residues –SH121 and S–S66-160 in the most open conformation were located at the opposite ends of the β-lac molecule. This would favour the intermolecular –SH/S–S interchange reactions that are known to occur in β-lac as part of the inter-molecular aggregation process. Furthermore, the unfolding of the β-lac increased the hydrogen bond forming capacity between water molecules and the protein and between water molecules themselves. The interactions and the properties of the water molecules in the protein hydration shell also indicated that the hydration shell was stabilized by protein unfolding. However, it was found that the unfolding of β-lac increased diffusion of hydration water molecules, including those in the first hydration shell that interact more strongly with the protein. This may partly explain why unfolded proteins are more likely to aggregate even though there were more hydration water molecules protecting them. Such results provided more detailed information on the structure-functionality relationship of β-lac based on both the protein molecule and its hydration shell. This provides insight into how we can control the processing of proteins for desirable functional properties such as thickening and gelation, which are modified through protein-water interactions.
Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.
Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Molecular simulation of partially denatured β-lactoglobulin
- Date Crossref
- 01/09/2023
- Éditeur
- Elsevier BV
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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Huazhong Agricultural University pays non établi dans la noticeUniversité ou école supérieure
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Heriot-Watt University pays non établi dans la noticeUniversité ou école supérieure
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Queen Margaret University pays non établi dans la noticeUniversité ou école supérieure
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Toronto Metropolitan University Department of Physics pays non établi dans la noticeUniversité ou école supérieure
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College of Food Science and Technology pays non établi dans la noticeUniversité ou école supérieure
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School of Engineering & Physical Sciences Institute of Mechanical pays non établi dans la noticeUniversité ou école supérieure
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School of Engineering and Physical Sciences Institute of Chemical Sciences pays non établi dans la noticeUniversité ou école supérieure
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Lab 13 Edinburgh Bioquarter pays non établi dans la noticeStructure de recherche
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School of Health Sciences pays non établi dans la noticeUniversité ou école supérieure
Huazhong Agricultural University, Heriot-Watt University et Queen Margaret University, avec 6 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.