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Updated: Jul 19, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Specificity of Prodan for the self-associating domain of spectrin: a molecular docking study
Malyasri Bhattacharya1, Chaitali Mukhopadhyay, Abhijit Chakrabarti
1Biophysics Division, Saha Institute of Nuclear Physics, 1/AF, Bidhannagar, Kolkata 700064 India.
Abstract:
The hydrophobic fluorescent probe Prodan binds to the self-associating domain of spectrin with 1:1 stoichiometry. A model of the self-associating domain was generated based on its homology with other domains of spectrin. Prodan was then docked onto the model, and several sites with low interaction energy were identified. To verify whether the binding of Prodan is specific towards the self-associating domain of spectrin, it was docked on to several other domains of spectrin, having a known three-dimensional structure. Analysis of the docking results suggests that the binding of Prodan to the self-associating domain of spectrin will involve hydrophobic and hydrophilic groups of Prodan. The results clearly indicate the preference of Prodan for a particular binding site of the self-associating domain.
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