Figure 3 | Scientific Reports

Figure 3

From: Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI)

Figure 3

Secondary and tertiary structural changes upon oxidative folding of NvCI. The secondary and tertiary structure changes along folding time were monitored by far-UV CD and tryptophan fluorescence spectra measurements, respectively. The fully reduced/unfolded protein was allowed to refold in 0.1 M Tris-HCl pH 8.4 at 20 °C. (a) Plot of ellipticity at 217 nm as a function of folding time. Inset: Far-UV CD spectra at different time points along folding. (b) Tryptophan spectrum area changes as a function of folding time. Inset: Tryptophan fluorescence spectra at different time points along folding. The arrow indicates the progression of the folding reaction along time.

Back to article page