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Figure 6 | BMC Biochemistry

Figure 6

From: Comparative thermodynamic studies on substrate and product binding of O-Acetylserine Sulfhydrylase reveals two different ligand recognition modes†

Figure 6

Dependence of ligand-OASS interactions on ionic strength-Fluorescence quenching titrations of ligands in the binding buffer with indicated [NaCl]. Solid line represents the fit derived from two identical site model; (A) Titrations of Cysteine with St OASS at indicated [NaCl] in the binding buffer; (closed square) 50 mM; (open circle) 100 mM; (open diamond) 200 mM; (closed triangle) 500 mM; (B) Titrations of methionine with St OASS at indicated [NaCl] in the binding buffer; (closed square) 100 mM; (open circle) 200 mM; (closed triangle) 500 mM; (C) Salt dependence of cysteine (closed circle) and methionine (open circle) binding constants. δlog(Kobs)/δlog[NaCl] ~ 0.8 for methionine binding.

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BMC Biochemistry

ISSN: 1471-2091

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