The thermodynamics of the unfolding of an isolated protein subdomain The 255–316 C-terminal fragment of thermolysin

Differential scanning calorimetry has been used to study the thermal unfolding of the 255–316 C-terminal fragment of thermolysin. The concentration effect on the calorimetric transitions of the fragment in 0.1 M NaCl and 20 mM phosphate buffer, pH 7.5, shows that it behaves as a highly stable dimer...

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