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Why the properties of proteins in salt solutions follow a Hofmeister series
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Theoretical Physics .
2004 (English)In: Current Opinion in Colloid & Interface Science, ISSN 1359-0294, E-ISSN 1879-0399, Vol. 9, no 01-Feb, 48-52 p.Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2004. Vol. 9, no 01-Feb, 48-52 p.
Keyword [en]
Hofmeister effect, ionic dispersion forces, lysozyme, salt solution
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-46181DOI: 10.1016/j.cocis.2004.05.001OAI: oai:DiVA.org:liu-46181DiVA: diva2:267077
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-13

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Boström, Mathias

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