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Updated: Apr 1, 2026

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
Fluorescence-Based Approaches for Quantitative Assessment of Protein Carbonylation, Protein Disulfides, and Protein
Asish R Chaudhuri1,2,3,4, Rochelle Wei5, Arunabh Bhattacharya5,6
1UT Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390, USA. asish.chaudhuri@utsouthwestern.edu.
Abstract:
Protein oxidation and misfolding have been considered as key players for progression of aging and etiology of various pathological conditions. However, few attempts have been made to develop sensitive and reproducible assays to quantify the changes in protein oxidation and alteration in structure. Here we describe three distinct fluorescence-based assays to quantify changes in protein oxidation, namely carbonylation and disulfides and alteration in protein surface hydrophobicity as a reporter for protein conformation. These techniques will provide investigators the opportunity to address important biological questions in their experimental models.
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