| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5400802 | Journal of Luminescence | 2013 | 9 Pages |
Abstract
⺠Binding of novel aminophosphinic acids with bovine serum albumin. ⺠Hydrophobic and hydrogen bonding attraction play major role in the binding process. ⺠Binding did not cause conformational changes in the protein. ⺠The quenching mechanism of fluorescence of BSA by aminophosphinic acids is a static quenching process.
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Authors
B. Kaboudin, K. Moradi, M.R. Faghihi, F. Mohammadi,