| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5401744 | Journal of Luminescence | 2012 | 6 Pages |
Abstract
⺠Interaction of TSFX and BSA was studied by multi-spectroscopic methods. ⺠Binding action was static quenching mainly by electrostatic interactions. ⺠Binding constant, number of binding sites and binding distance were calculated. ⺠TSFX changed the conformation and secondary structure of BSA. ⺠With TSFX the polarity of Trp micro-region increased and the polypeptides unfolded.
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Authors
Fengyu Deng, Ying Liu,