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. Author manuscript; available in PMC: 2009 Sep 2.
Published in final edited form as: Biochemistry. 2008 Aug 9;47(35):9227–9233. doi: 10.1021/bi801102e

Figure 4.

Figure 4

Temperature dependence of the conformational exchange kinetics in E:THF:NADP+ at pH 7.6 for the (A) active-site loops and (B) C-terminal associated region. Rate constants for the excited-to-ground state (kBA; ■) and ground-to-excited state (kAB; ▲) transitions, and the equilibrium constant (kBA/kAB;●) are plotted. (C) Thermodynamic comparison of E:FOL:NADP+ and E:THF:NADP+ at 298 K. Thermodynamic barriers were calculated using transition-state theory according to Materials and Methods. Green, blue and red traces represent DG, DH and TDS respectively. E:FOL:NADP+ is a model for the Michaelis complex E:DHF:NADPH.