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. 2001 May 15;98(11):6127–6131. doi: 10.1073/pnas.111157998

Table 2.

Properties of the pH-induced unfolding reactions in citrate vs. acetate buffer

Citrate Acetate
Protein pHm ΔGNI pHm ΔGNI
WT 4.7 4.8 4.4 7.0
H24V/H119F 3.5* 7.2 3.2 8.2
H36Q n.d. n.d. 5.3 5.3

Determined at 4.5°C in either 10 mM acetate or 2 mM citrate, 30 mM NaCl buffer. pHm is the pH midpoint of the unfolding transition monitored by the final fluorescence values obtained in unfolding/refolding experiments, as in Fig. 4 A and B. ΔGNI is the Gibbs energy difference between the native and molten globule forms at pH 9, in kcal/mol, computed from the values of ku and kf used to fit the curve of log kobs vs. pH. 

*

A lower value than the one given here is obtained if the baseline found for the WT protein is used.