*2.3. Synchronous Fluorescence*

Synchronous fluorescence spectrometry is used as a common tool to inspect conformational changes in proteins in the presence of other molecules, also termed quenchers [39]. Synchronous fluorescence analysis of α-amylase was carried out in the absence and presence of caffeic acid and coumaric acid (0–20 µM) to obtain the spectra. A 15 nm difference was kept for Tyr residues between the excitation (245 nm) and emission spectra (260–340 nm). In a similar manner for Trp, the difference was maintained at 60 nm, the excitation was fixed at 220 nm and the emission was between 280–400 nm.
