Skip to main content
Fig. 2 | BMC Microbiology

Fig. 2

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. 2

Nucleotide binding affinities of a HpMutS2 b HpMutS2-G338R and c HpMutS2-E413A. Tryptophan fluorescence assays described in the Methods section were used to determine the nucleotide binding affinities of proteins. The dissociation constants were calculated by non-linear regression analysis of plots of ΔF/ΔFmax versus the ligand concentration. ΔF: magnitude of the difference between the observed fluorescence intensity at a given ligand concentration and the fluorescence intensity in the absence of any ligand, ΔFmax: difference at an infinite ligand concentration

Back to article page

BMC Microbiology

ISSN: 1471-2180

Contact us