Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori

Figure 5

Thermal unfolding of H. pylori enolase. (a) Unfolding transitions of apo- and holoenolase from H. pylori monitored by CD spectroscopy at 220 nm; the experiments were carried out in 50 mMTris-HCl buffer at pH 7.4. Blue line: apo-HpEno, green line: holo-enolase (Mg⁺ 2 mM), black line: apo-ScEno, and red line: holo-ScEno (Mg⁺ 2 mM). (b) Kinetics of the thermal denaturation curves of holo-HpEno at different heating rates. The denaturation process was monitored by recording the ellipticity at 220 nm at a constant temperature. The insets correspond to the plots ofln(k₁/T) versus 1/T, which represents the Eyring equation.

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