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Dar TA, Singh LR, Islam A, Anjum F, Moosavi-Movahedi AA, Ahmad F
Guanidinium chloride and urea denaturations of beta-Lactoglobulin A at pH 2.0.and 25 degrees C: The equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches)
Biophysical Chemistry (2007) 127:140-148.
Abstract
We have carried out guanidinium chloride (GdmCl) and urea denaturations of bovine beta-lactoglobulin A (beta-lgA) at pH 2.0 and 25 degrees C, using far-UV and near-UV circular dichroism, near-UV absorption and tryptophan fluorescence spectroscopies. The stable intermediate state that occurs during GdmCl denaturation has been characterized by the far- and near-UV circular dichroism, tryptophan difference absorption, tryptophan fluorescence and 8-anilino-1-naphthalene sulphonic acid binding measurements. Following conclusions have been reached. (a) Urea-induced denaturation is not a two-state process. (b) GdmCl-induced denaturation is composed of two distinct two-state processes. (c) alpha-Helical content, burial of tryptophan residues and burial of hydrophobic surface area are more in the GdmCl-induced stable intermediate than those originally present in the native protein. (c) 2007 Elsevier B.V. All rights reserved.
Note
Publication Date: 2007-05-01.
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