| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5401837 | Journal of Luminescence | 2012 | 8 Pages |
Abstract
⺠GA binds to Sudlow's site II in BSA and form a 1:1 complex with it. ⺠GA quenches the fluorescence of BSA in a static profile. ⺠Main hydrophobic forces and binding distance between them are determined. ⺠GA binding results in an increased hydrophobicity around tryptophans in BSA. ⺠GA binding causes a decrease in α-helix and an increase in β-sheet substructures.
Keywords
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Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Wei Du, Teng Teng, Chen-Chen Zhou, Lei Xi, Jing-Zhang Wang,