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. 2014 Dec 31;9(12):e115941. doi: 10.1371/journal.pone.0115941

Figure 2. Fluorescence quenching of NS3 Trp residues by acrylamide at pH 6.4 and 7.2.

Figure 2

Acrylamide concentrations ranging from 0 to 156 mM were used to monitor the exposure of the Trp residues of NS3hel (A) and NS3FL (B) at pH 6.4 (closed circles) and 7.2 (open circles) and to calculate the Stern-Volmer constant (Ksv) using Equation 3 (Material and Methods). Each point corresponds to the mean of tryptophan fluorescence quenching by acrylamide obtained in three independent experiments. Spectra were acquired at 25°C in buffer solutions composed of 50 mM MOPS-NaOH (pH 6.4 or 7.2), 200 mM NaCl, 5 mM β-mercaptoethanol and 5% glycerol. The protein concentration was 1 µM.