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C. N. Pace, E. J. Hebert, K. L. Shaw, D. Schell, V. Both, D. Krajcikova, J. Sevcik, K. S. Wilson, Z. Dauter, R. W. Hartley and G. R. Grimsley, “Conformational Stability and Thermodynamics of Folding of Ribonucleases Sa, Sa2 and Sa3,” Journal of Molecular Biology, Vol. 279, No. 1, 1998, pp. 271-286. doi:10.1006/jmbi.1998.1760
has been cited by the following article:
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TITLE:
Pressure- and Urea-Induced Denaturation of Bovine Serum Albumin: Considerations about Protein Heterogeneity
AUTHORS:
Douglas Ricardo Norberto, Joelma Mauricio Vieira, Ancelmo Rabelo de Souza, Jose Ailton Conceicao Bispo, Carlos Francisco Sampaio Bonafe
KEYWORDS:
Apparent Stoichiometric Coefficient; Bovine Serum Albumin; High Pressure-Induced Denaturation; Protein Heterogeneity; Urea-Induced Denaturation
JOURNAL NAME:
Open Journal of Biophysics,
Vol.2 No.1,
January
19,
2012
ABSTRACT: Urea denatures proteins at different concentrations, depending on the experimental conditions and the protein. We in-vestigated the pressure-induced denaturation of bovine serum albumin (BSA) in the presence of subdenaturing concen-trations of urea based on a two-state equilibrium. Pressure-induced denaturation was enhanced at urea concentrations ([U]) of 3.5 M to 8.0 M, with the free energy of denaturation at atmospheric pressure ranging from +5.0 to –2.5 kJ/mol of BSA. The m values appeared to be biphasic, with m1 and m2 of 0.92 and 2.35 kJ mol–1?M–1, respectively. Plots of versus ln[U] yielded values of u, the apparent stoichiometric coefficient, of 1.68 and 6.67 mol of urea/mol of BSA for m1 and m2, respectively. These values were compared with the m and u values of other monomeric proteins reported in or calculated from the literature. The very low values of u systematically observed for proteins were suggestive of heterogeneity in the free energy of denaturation. Thus, a u value of 140 mol of urea/mol of BSA may indicate the existence of a heterogeneous molecular population with respect to the free energy of dena-turation.