Biophysical Studies on the Interactions of a Classic Mitochondrial Uncoupler with Bovine Serum Albumin by Spectroscopic, Isothermal Titration Calorimetric and Molecular Modeling Methods

@article{Zhang2010BiophysicalSO,
  title={Biophysical Studies on the Interactions of a Classic Mitochondrial Uncoupler with Bovine Serum Albumin by Spectroscopic, Isothermal Titration Calorimetric and Molecular Modeling Methods},
  author={Yue Zhang and Jia-Han Li and Yu-Shu Ge and X Liu and Feng-Lei Jiang and Yi Liu},
  journal={Journal of Fluorescence},
  year={2010},
  volume={21},
  pages={475-485}
}
The interaction between a classic uncoupler (2,4-dinitrophenol, DNP) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy under the physiological conditions. The fluorescence quenching constants were calculated by the Stern-Volmer equation, and based upon the temperature dependence of quenching constants, it was proved that DNP caused a static quenching of the intrinsic fluorescence of BSA. Owing to the static quenching mechanism, different associative binding constants… CONTINUE READING

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