- Exposure of thiol groups in the heat-induced denaturation of β-lactoglobulin
- Molecular Simulation
- Volume | Issue number
- 41 | 10-12
- Pages (from-to)
- Document type
- Faculty of Science (FNWI)
- Van 't Hoff Institute for Molecular Sciences (HIMS)
Protein aggregates can be stabilized by disulfide bridges. The whey protein β-lactoglobulin (β-lac) contains a disulfide bridge and a free cysteine that are shielded from the solvent by an α-helix. These groups are important in the thiol-disulfide exchange that occurs during aggregation and gelation of β-lac. Replica exchange mol. dynamics simulations show that the exposure mechanism is very different for the 2 buried groups. While melting of the α-helix enhances exposure of the free cysteine, it does not for the buried bridge. These findings shed light on the mol. mechanism of the first step of β-lac denaturation and aggregation.
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