Apomyoglobin stability as dependent on urea concentration and temperature at two pH values

Equilibrium unfolding of apomyoglobin (ApoMb) in the presence of urea was studied as dependent on the temperature (5–2°C) at two pH values (5.7 and 6.2). Thermodynamic parameters of ApoMb transition from the native to the unfolded state were estimated under various conditions. Conformational changes in ApoMb were detected by tryptophan fluorescence and far-UV circular dichroism. The ApoMb stability and the cooperativity of its unfolding at 5°C were considerably lower than at other temperatures at both pH values, where ApoMb is in the native conformation.__________Translated from Molekulyarnaya Biologiya, Vol. 39, No. 2, 2005, pp. 330–335.Original Russian Text Copyright © 2005 by Baryshnikova, Sharapov, Kashparov, Ilyina, Bychkova.