Title : Effect of Ligands on HP-Induced Unfolding and Oligomerization of β-Lactoglobulin.

Pub. Date : 2020 Dec 1

PMID : 33129832






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Bovine beta-lactoglobulin (BLG), the main whey protein, has a strong propensity to bind various bioactive molecules, such as retinol and resveratrol, two ligands with different affinity and binding sites. Vitamin A beta-lactoglobulin Bos taurus
2 Bovine beta-lactoglobulin (BLG), the main whey protein, has a strong propensity to bind various bioactive molecules, such as retinol and resveratrol, two ligands with different affinity and binding sites. Vitamin A beta-lactoglobulin Bos taurus
3 Retinol, which has a high affinity for BLG hydrophobic cavity, significantly stabilizes BLG both in 3D and local environments, by shifting the onset of protein unfolding by ~100 MPa. Vitamin A beta-lactoglobulin Bos taurus
4 Retinol, which has a high affinity for BLG hydrophobic cavity, significantly stabilizes BLG both in 3D and local environments, by shifting the onset of protein unfolding by ~100 MPa. Vitamin A beta-lactoglobulin Bos taurus
5 Ab initio modeling of SANS shows that the oligomers formed from BLG/retinol complex are smaller and more elongated compared to BLG without ligand or in the presence of resveratrol. Vitamin A beta-lactoglobulin Bos taurus
6 Ab initio modeling of SANS shows that the oligomers formed from BLG/retinol complex are smaller and more elongated compared to BLG without ligand or in the presence of resveratrol. Vitamin A beta-lactoglobulin Bos taurus