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Figure 4
CD spectroscopy on RepA–WT and its fragments. (A) CD spectra (260–195 nm range) were acquired at 5°C, for stocks of each protein (6–25  M). Spectra are plotted to the same scale in mean molar ellipticity per residue ( MR) units (deg.cm2.dmol-1). The inset to the figure shows the symbols used to plot each protein spectrum. Structural changes associated with RepA monomerization are evident (see text). (B) Thermal denaturation profiles. The same samples studied in (A) were then heated from 5 to 90°C, measuring the evolution of the ellipticity at 222 nm ( -helix signature). Data were plotted as MR222 (deg.cm2.dmol-1) versus temperature (°C). The inset shows the symbols used to mark the curve for each protein sample, together with its calculated melting temperature (Tm, 50% unfolding). These plots are compatible with the existence in RepA of two stable folding units (two globular domains).
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