Structure-energetics relationships for thermal denaturion of holo- and apo-AGT enzymes.

<p>A) Temperature dependence of denaturation enthalpies (Δ<i>H</i>) for holo- (closed symbols) and apo-(open symbols) proteins. The linear fit provides the value of ΔC_p ( = 10.2±0.6 kcal.mol⁻¹). B) Activation energy (<i>E</i>_a) plotted vs. the <i>T</i>_m for holo- (closed symbols) and apo-(open symbols) AGT enzymes. C and D) changes in activation enthalpic and entropic contributions to AGT kinetic stability as a function of changes in activation free energies for holo-(C) and apo-(D) AGT enzymes. Lines in C and D are meant to guide the eye and have no theoretical meaning.