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![[Figure 2]](ts5020fig2mag.jpg)
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Figure 2
Characterization of the 2-Helix protein. (a) SDS–PAGE analysis of the proteins. 2-Helix protein was expressed as a GST-fusion protein and cleaved by GST-3C enzyme. Lane M, protein molecular-weight markers in kDa as indicated; lane 2, purified GST control protein; lane 3, 2-Helix protein after GST-3C cleavage; lane 4, purified GST-fusion 2-Helix. (b) MALDI–TOF mass-spectrometry profile of the 2-Helix. It is clearly shown that the molecular weight of the major peak is 9.718 kDa, matching the molecular weight of the 2-Helix monomer. (c) Gel-filtration analysis of the 2-Helix protein. In the Superdex G75 column elution pattern, a clear peak between the eluted volumes corresponding to 52 and 14.4 kDa standards indicates the 2-Helix protein. It is of about 30 kDa in weight, indicating the formation of a 2-Helix trimer or six-helix bundle. The inset picture is Tris–tricine SDS–PAGE analysis of the peak, indicating the existence of only 2-Helix protein in the peak. The molecular standards run are indicated in kDa. (d) CD spectra of the 2-Helix protein. A typical α-helix secondary structure with double minima at 208 and 222 nm was seen for the 2-Helix protein sample. |
![[Figure 2]](ts5020fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
