Interaction of bovine serum albumin with dipolar molecules: fluorescence and molecular docking studies.

@article{Bhattacharya2009InteractionOB,
  title={Interaction of bovine serum albumin with dipolar molecules: fluorescence and molecular docking studies.},
  author={Bhaswati Bhattacharya and Srinivas Nakka and Lalitha Guruprasad and Anunay Samanta},
  journal={The journal of physical chemistry. B},
  year={2009},
  volume={113 7},
  pages={2143-50}
}
Interaction of bovine serum albumin (BSA) with two series of dipolar molecules having both rigid and flexible structures has been studied by monitoring the spectral and temporal behavior of the intramolecular charge transfer fluorescence of the systems. The binding sites of the molecular systems in BSA have been located with the help of docking studies. Three different sites of varying hydrophobicity have been identified where these molecules are located. Binding in the hydrophobic domains of… CONTINUE READING
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