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Figure 4 | BMC Biochemistry

Figure 4

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

Figure 4

ITC analysis of the interaction between OASS and cysteine. Data is plotted as heat signal (μJ/sec) versus time (min) in the upper panel in each fig. Lower panel-Integrated heat responses per injection from panel A plotted as normalized heat per mole of injectant. The solid line represents the best fit of the data to a two independent site binding model (eqn 2). (A) Titration of St OASS (4.5 μM) with cysteine (350 mM) at 25°C. (B) Titration of St OASS (4.5 μM) with Methionine (350 mM) at 25°C. (C) Titration of Mt OASS (4.5 μM) with Cysteine (350 mM) at 25°C. (D) Titration of Hi OASS (4.5 μM) with cysteine (350 mM) at 25°C.

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BMC Biochemistry

ISSN: 1471-2091

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