The thermal stabilities of dimeric bovine β-lactoglobulin and monomeric equine β-lactoglobulin were investigated at neutral pH by means of differential scanning calorimetry, circular dichroism, tryptophan fluorescence, and by binding of an hydrophobic probe. Differential scanning calorimetry showed the presence of two structural domains with different thermal stabilities in both proteins. Thermodynamic analysis of the calorimetric signal revealed that the two domains unfold independently according to a mechanism where an equilibrium step is followed by an irreversible transition. The spectroscopic data supported this model and allowed recognition of the structural regions corresponding to the more thermally stable domain. The differences in thermal stability between the two proteins can be primarily ascribed to the properties of the less stable domain.

Thermal unfolding of monomeric and dimeric beta-lactoglobulins / D. Fessas, S. Iametti, A. Schiraldi, F. Bonomi. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 268:20(2001), pp. 5439-5448.

Thermal unfolding of monomeric and dimeric beta-lactoglobulins

D. Fessas
Primo
;
S. Iametti
Secondo
;
A. Schiraldi
Penultimo
;
F. Bonomi
Ultimo
2001

Abstract

The thermal stabilities of dimeric bovine β-lactoglobulin and monomeric equine β-lactoglobulin were investigated at neutral pH by means of differential scanning calorimetry, circular dichroism, tryptophan fluorescence, and by binding of an hydrophobic probe. Differential scanning calorimetry showed the presence of two structural domains with different thermal stabilities in both proteins. Thermodynamic analysis of the calorimetric signal revealed that the two domains unfold independently according to a mechanism where an equilibrium step is followed by an irreversible transition. The spectroscopic data supported this model and allowed recognition of the structural regions corresponding to the more thermally stable domain. The differences in thermal stability between the two proteins can be primarily ascribed to the properties of the less stable domain.
β-lactoglobulin; DSC; Protein thermal stability; Spectroscopy
Settore CHIM/02 - Chimica Fisica
Settore BIO/10 - Biochimica
2001
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/6545
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