Flow Induced Dispersion Analysis (FIDA), based on Taylor dispersion analysis, can quantify protein structural stability and unfolding using only 40 ng of protein per data point. Using a Fida 1 instrument with UV-LED intrinsic fluorescence detection, the authors introduced a "capillary mixing" mode in which a protein sample is dispersed into a guanidinium chloride denaturant solution inside the capillary, removing the need for a manual dilution series. Each measurement simultaneously reports hydrodynamic radius and intrinsic fluorescence, revealing unfolding as the denaturant increases from 0 to 6 M. The method characterized the antibody adalimumab and human serum albumin across pH 4, 7 and 10, yielding denaturation midpoints (Cm) and Gibbs free energy of unfolding (ΔG°). The automated, in-solution, label-free workflow takes about 6 minutes per point, well suited to early drug development or scarce samples.