1992 Volume 40 Issue 2 Pages 504-505
The denaturation of the 57kilodalton (kDa) rat liver nuclear thyroid hormone binding protein (NTHB) by pH and guanidine hydrochloride (GdnHCl) has been investigated with the fluorescence method. The acid and alkaline fluorescence quenching suggests that the structure of NTHB is invariant in the relatively narrow pH region of approximately pH 7-9. A cooperative conformational transition occured in GdnHCl concentrations of 1.5-2.5M. The apparent free energy of unfolding of NTHB, ΔGH2Oapp was evaluated as 6.31 (±0.12) kcal·mol-1 at pH 7.7, 25°C.