Sj. Bae et Jm. Sturtevant, THERMODYNAMICS OF THE THERMAL UNFOLDING OF EGLIN-C IN THE PRESENCE AND ABSENCE OF GUANIDINIUM CHLORIDE, Biophysical chemistry, 55(3), 1995, pp. 247-252
The thermal unfolding of eglin c, a small proteinase inhibitor of mole
cular weight 8.1 kDa, is studied by means of high sensitivity scanning
calorimetry over a wide pH range in dilute buffer solutions, and in t
he presence of varying concentrations of guanidinium chloride at pH 7.
00 and 10.55. The temperature of half-completion of the unfolding tran
sition, t(1/2), in dilute buffer varies from 41 degrees C at pH 1.1 to
86 degrees C at pH 7.0 to 10.55, with corresponding enthalpy changes
of approximately 40 kcal mol(-1) and 71 kcal mol(-1). This latter enth
alpy change, amounting to 8.7 cal g(-1), is unusually large for a prot
ein, especially for one of unusually small molecular weight. Addition
of 3.3 M guanidinium chloride at pH 10.55 lowered t(1/2) from 86 degre
es C to 40 degrees C and decreased the enthalpy change from approximat
ely 71 kcal mol(-1) to 25 kcal mol(-1).