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![[Figure 2]](yt5033fig2mag.jpg)
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Figure 2
T-ag OBD Cys216A mutant is monomeric in solution. Results of Cu(1,10-phenanthroline)2SO4 (CuP) catalyzed oxidation experiments electrophoresed on an SDS–polyacrylamide gel and stained with Coomassie Brilliant Blue. Lane 4 contains molecular-weight markers (250, 150, 100, 75, 50, 37, 25, 20, 15 and 10 kDa). Lanes 1–3 contain wt T-ag OBD and lanes 5–7 contain the C216A mutant protein. Lanes 2 and 6 show the results of CuP oxidation and lanes 3 and 7 show the results of oxidation with CuP followed by treatment with the reducing agent DTT. These data show that under oxidizing conditions the wt OBD forms dimers, whereas the C216A mutant remains monomeric. |
![[Figure 2]](yt5033fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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