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Fig. 3 | BMC Microbiology

Fig. 3

From: Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function

Fig. 3

Mutation induced conformational changes in HpMutS2. a CD-spectroscopy of HpMutS2, HpMutS2-G338R, and HpMutS2-E413A. Far-UV CD spectra of proteins (1 μM) dialyzed in 50 mM Tris-Cl and 100 mM NaCl were recorded between 200–300 nm with 20 mdeg sensitivity at a scan speed of 50 nm using 2 mm path length cuvette with a bandwidth of 2 nm. The spectra were recorded using Jasco-815 spectropolarimeter. Size exclusion chromatographic analysis of b HpMutS2, c HpMutS2-G338R, and d HpMutS2-E413A was performed using Superose-6 gel filtration column at a constant flow rate of 0.3 ml/min. Approximately 150 μg of all the proteins were spun at 10,000 rpm for 10 min at 4 °C before injection. The absorbance was recorded at 280 nm

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