Before revision:  While increasing the applied tip force from 6 to 12 nN did not significantly change the temperature dependence of ETp via apo-Az, ETp via holo-Az changed qualitatively, namely from temperature-independent at 6 nN to thermally activated at forces \geq 9 nN, suggesting changes in the protein structure upon increasing the applied force. The capability of exploring ETp by CP-AFM  over a significant range of temperatures, with varying tip force to detect possible pressure-induced changes in the sample , significantly adds to the ability to study ETp through proteins and of using ETp to study proteins, with this approach .
After revision:  While increasing the applied tip force from 6 to 12 nN did not significantly change the temperature dependence of ETp via apo-Az, ETp via holo-Az changed qualitatively, namely from temperature-independent and thermally activated via apo-Az. This observation agrees with macroscopic-scale measurements, thus confirming that the difference in ETp dependence on temperature between holo- and apo-Az is an inherent one that may reflect a difference in rigidity between the two forms. An important implication of these results, which depend on CP-AFM over a significant range of temperatures, with varying tip force to detect possible pressure-induced changes in the sample , significantly adds to the ability to study ETp through proteins and of using ETp to study proteins, with this approach .