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

M. Boström; D. R.M. Williams; B. W. Ninham

doi:10.1016/j.cocis.2004.05.001

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

M. Boström^*, D. R.M. Williams, B. W. Ninham

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

72 Citations (Scopus)

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.

Original language	English
Pages (from-to)	48-52
Number of pages	5
Journal	Current Opinion in Colloid and Interface Science
Volume	9
Issue number	1-2
DOIs	https://doi.org/10.1016/j.cocis.2004.05.001
Publication status	Published - Aug 2004

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10.1016/j.cocis.2004.05.001

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title = "Why the properties of proteins in salt solutions follow a Hofmeister series",

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.",

keywords = "Hofmeister effect, Ionic dispersion forces, Lysozyme, Salt solution",

author = "M. Bostr{\"o}m and Williams, {D. R.M.} and Ninham, {B. W.}",

year = "2004",

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AU - Boström, M.

AU - Williams, D. R.M.

AU - Ninham, B. W.

PY - 2004/8

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N2 - 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.

AB - 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.

KW - Hofmeister effect

KW - Ionic dispersion forces

KW - Lysozyme

KW - Salt solution

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DO - 10.1016/j.cocis.2004.05.001

M3 - Article

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EP - 52

JO - Current Opinion in Colloid and Interface Science

JF - Current Opinion in Colloid and Interface Science

IS - 1-2

ER -

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

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