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  • Title: The thermodynamics of the unfolding of an isolated protein subdomain. The 255-316 C-terminal fragment of thermolysin.
    Author: Conejero-Lara F, De Filippis V, Fontana A, Mateo PL.
    Journal: FEBS Lett; 1994 May 16; 344(2-3):154-6. PubMed ID: 8187875.
    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, within the concentration range 0.19-4.55 mg/ml, undergoing a reversible two-state thermal unfolding process. The thermodynamic parameters of unfolding (delta G = 60 +/- 6 kJ/(mol of dimer) at 20 degrees 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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