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A direct calorimetric determination of denaturation enthalpy for lysozyme in sodium dodecyl sulfate.
Behbehani, G Rezaei; Saboury, A A; Taleshi, E.
Afiliação
  • Behbehani GR; Chemistry Department, Imam Khomeini International University, Qazvin, Iran. grb402003@yahoo.com
Colloids Surf B Biointerfaces ; 61(2): 224-8, 2008 Feb 15.
Article em En | MEDLINE | ID: mdl-17889513
Thermodynamics of the interaction between sodium dodecyl sulfate (SDS) with lysozyme were investigated at pH 7.0 and 27 degrees C in phosphate buffer by isothermal titration calorimetry. A new method to follow protein denaturation, and the effect of surfactants on the stability of proteins was introduced. The new solvation model was used to reproduce the enthalpies of lysozyme-SDS interaction over the whole range of SDS concentrations. The solvation parameters recovered from the new equation, attributed to the structural change of lysozyme and its biological activity. At low concentrations of SDS, the binding is mainly electrostatic, with some simultaneous interaction of the hydrophobic tail with nearby hydrophobic patches on the lysozyme. These initial interactions presumably cause some protein unfolding and expose additional hydrophobic sites. The enthalpy of denaturation is 160.81+/-0.02 kJ mol(-1) for SDS.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Desnaturação Proteica / Dodecilsulfato de Sódio / Calorimetria / Muramidase Limite: Animals Idioma: En Ano de publicação: 2008 Tipo de documento: Article
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Desnaturação Proteica / Dodecilsulfato de Sódio / Calorimetria / Muramidase Limite: Animals Idioma: En Ano de publicação: 2008 Tipo de documento: Article