• Title of article

    Hofmeister effects: Why protein charge, pH titration and protein precipitation depend on the choice of background salt solution

  • Author/Authors

    Moreira، نويسنده , , L.A. and Bostrِm، نويسنده , , M. and Ninham، نويسنده , , B.W. and Biscaia، نويسنده , , E.C. and Tavares، نويسنده , , F.W.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2006
  • Pages
    7
  • From page
    457
  • To page
    463
  • Abstract
    Protein solubility, protein charge and acid–base titration in protein solutions depend strongly on the choice of background salt solution. Hofmeister effects, or sequences, refer to the relative effectiveness of anions or cations on a wide range of phenomena. Understanding this ion specificity is vital for biology, biotechnology, and colloid chemistry but the reason has, until very recently, not been clear. We present calculations using the Poisson–Boltzmann equation that includes not only electrostatic interactions but also many-body ion–protein dispersion potentials, originated from polarizabilities of ions and proteins. These calculations reveal that is possible to qualitatively predict different Hofmeister effects observed in protein solutions. Our results enable us to give an explanation for the Hofmeister series observed in the measured pH in protein and buffer solutions, protein charge and ion adsorption on protein surface.
  • Keywords
    Poisson–Boltzmann equation , Hofmeister effect , polarizability , Ionic dispersion potentials , cytochrome c
  • Journal title
    Colloids and Surfaces A Physicochemical and Engineering Aspects
  • Serial Year
    2006
  • Journal title
    Colloids and Surfaces A Physicochemical and Engineering Aspects
  • Record number

    1792672