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. Study holds ProTherm entries: 10548, 10549, 10550, 10551, 10552, 10553, 10554, 10555 Extra Details: 255-316 C-terminal fragment differential scanning calorimetry; thermolysin; protein stability;,protein domain; domain folding

Submission Details

ID: WNzjPM7h3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details

Conejero-Lara F;De Filippis V;Fontana A;Mateo PL,FEBS Lett. (1994) The thermodynamics of the unfolding of an isolated protein subdomain. The 255-316 C-terminal fragment of thermolysin. PMID:8187875

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