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![[Figure 2]](cb5132fig2mag.jpg)
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Figure 2
Characterization of SmeCOSe samples. (a) SEC experiments carried out with SmeCOSe in 20 mM Tris–HCl pH 8.0 at three concentrations (solid black line and dashed lines). Thyroglobulin (660 kDa), glucose isomerase (173 kDa) and ovoalbumin (45 kDa) standards are also shown. The inset represents the fitting used to estimate the oligomerization of SmeCOSe (black point; estimated molecular mass of 201 ± 6 kDa). (b) Effect of pH on the apparent thermal denaturation midpoint of SmeCOSe (red symbols, left axis) and the raw ellipticity at 222 nm, which is indicative of α-helical secondary structure (far UV-CD, black diamonds, right axis). (c) TSA experiments showing the increase in the ![[T_{\rm m}^{\rm app}]](teximages/cb5132fi1.svg) of the C54S SmeCOSe mutant in the presence of choline-O-sulfate and choline. |
![[Figure 2]](cb5132fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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