Investigating MLGI kinetics by QD-FRET. FRET signals induced by QD-DiMan-lectin binding were further employed to measure the binding kinetics by stopped flow fluorescence. The association rate was obtained by rapid mixing QD-DiMan and labeled lectin into an 80 µL cuvette at a 1:1 molar ratio via stopped flow apparatus. Measurements were background corrected and the averaged FRET ratiotime profiles were fitted by the second order rate equation to derive the apparent on-rate coefficient, 𝑘 𝑜𝑛 (Eq. 4), where, 𝑥 0 is the initial protein concentration and 𝑎 is a constant which accounts for fluorescence degradation.