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Fig. 4 | BMC Microbiology

Fig. 4

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. 4

Nucleotide and mutation induced conformational changes in HpMutS2. a Limited proteolysis. Proteins (4 μM) either free or pre-incubated with nucleotides (1 mM) were incubated with chymotrypsin (1.25 ng) for 30 min at 37 °C. All proteolysis reactions were performed in 1X buffer A lacking magnesium. Reactions were stopped by adding a protease inhibitor cocktail and the products were separated on SDS-PAGE (10 %). Lane M: Molecular weight marker. b Thermal stability profiles of wild-type HpMutS2, HpMutS2-G338R, and HpMutS2-E413A. Proteins (1 μM) dialyzed in 50 mM Tris-Cl and 100 mM NaCl were subjected to thermal denaturation and spectra were recorded at 222 nm using Jasco-815 spectropolarimeter

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