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Cation specific binding with protein surface charges
2009 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 106, no 32, 13296-300 p.Article in journal (Refereed) Published
Abstract [en]

Biological organization depends on a sensitive balance of noncovalent interactions, in particular also those involving interactions between ions. Ion-pairing is qualitatively described by the law of "matching water affinities." This law predicts that cations and anions (with equal valence) form stable contact ion pairs if their sizes match. We show that this simple physical model fails to describe the interaction of cations with (molecular) anions of weak carboxylic acids, which are present on the surfaces of many intra- and extracellular proteins. We performed molecular simulations with quantitatively accurate models and observed that the order K(+) < Na(+) < Li(+) of increasing binding affinity with carboxylate ions is caused by a stronger preference for forming weak solvent-shared ion pairs. The relative insignificance of contact pair interactions with protein surfaces indicates that thermodynamic stability and interactions between proteins in alkali salt solutions is governed by interactions mediated through hydration water molecules.

Place, publisher, year, edition, pages
2009. Vol. 106, no 32, 13296-300 p.
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Physical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-82976DOI: 10.1073/pnas.0902904106ISI: 000268877300029PubMedID: 19666545OAI: oai:DiVA.org:kth-82976DiVA: diva2:498632
Note
QC 20120217Available from: 2012-02-12 Created: 2012-02-12 Last updated: 2017-12-07Bibliographically approved

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Hess, Berk

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