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Figure 3
T-ag OBD double mutants primarily form dimers. Results of Cu(1,10-phenanthroline)2SO4 (CuP) catalyzed oxidation experiments electrophoresed on an SDS-polyacrylamide gel and stained with Coomassie Brilliant Blue. Lane 3 contains molecular-weight markers (250, 150, 100, 75, 50, 37, 25, 20, 15 and 10 kDa). Lanes 1–2 show C216A, F151C mutant OBD and lanes 4–5 show C216A, D256C mutant protein. Lanes 1 and 4 show the results of CuP oxidation and lanes 2 and 5 show the results of overnight dialysis in reaction buffer (no reducing agent). These data show that under oxidizing conditions the double mutants form dimers, unlike the single C216A mutant.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 67| Part 6| June 2011| Pages 560-567
https://doi.org/10.1107/S0907444911014302
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