Why the properties of proteins in salt solutions follow a Hofmeister series

Bostroem, M. and Williams, D. R. M. and Ninham, B. W. (2004) Why the properties of proteins in salt solutions follow a Hofmeister series. CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 9 (1-2). pp. 48-52. ISSN 1359-0294, 1879-0399

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Abstract

The physical properties of hen-egg-white lysozyme, and other globular protein, in aqueous solutions depend in a complicated and unexplained way on pH, salt type and salt concentration. One important and previously neglected source of ion specificity is the ionic dispersion potential that acts between each ion and the protein. We present model calculations, performed within a modified ion-specific double layer theory, that demonstrate the large effect of including these ionic dispersion potentials. (C) 2004 Elsevier Ltd. All rights reserved.

Item Type: Article
Uncontrolled Keywords: ION SPECIFICITY; ELECTROLYTE-SOLUTIONS; DISPERSION FORCES; CO-IONS; BINDING; POTENTIALS; LYSOZYME; CHARGE; ANION; WATER; Hofmeister effect; ionic dispersion forces; lysozyme; salt solution
Subjects: 500 Science > 540 Chemistry & allied sciences
Divisions: Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie
Depositing User: Petra Gürster
Date Deposited: 25 Jan 2022 11:29
Last Modified: 25 Jan 2022 11:29
URI: https://pred.uni-regensburg.de/id/eprint/37374

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