The secondary structure of a major wine protein is modified upon interaction with polyphenols - Supplemnetary

Figure S1: Plot of secondary structure content of VVTL1 alone or in presence of 2 eq. of polyphenols (indicated) versus temperature. Secondary structure content was determined from SRCD data by CDApps [46] using CONTINLL algorithm [47]. VVTL1 concentration was 0.400 mg/mL. Figure S2: Melting curves of VVTL1 alone or in presence of 2 eq. of polyphenols (indicated). Curves were obtained plotting the ΔSRCD signal at 195 nm of VVTL1 versus temperature. Figure S3: Far-UV SRCD spectra (20 repeated scans collected at 20°C) of VVTL1 alone or in presence of different polyphenols. SRCD spectra were recorded using a Suprasil 0.02 cm cell (Hellma) filled with 60 µL of solution, integration time 1 s, 1 nm digital resolution, 39 nm/min scan speed and monochromator slit widths to 1.2 nm bandwidth. Protein concentration 0.400 mg/mL in MWS. Figure S4: Changes in the SRCD signal at 195 nm versus the number of scans of VVTL1 alone and in presence of polyphenols (indicated).