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

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Abstract
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 in solution, whithin the concentration range 0.19–4.55 mg/ml, undergoing a reversible two‐state thermal unfolding process. The thermodynamic parameters of unfolding (ΔG = 60 ± 6 kJ/(mol of dimer) at 20°C) are similar to those normally observed for small, compact, globular proteins. This and previous studies [1989, Eur. J. Biochem. 180, 513–518] show that the 255–316 fragment folds into a stable, native‐like globular structure.

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