- Title
- Decomposing Hofmeister effects on amino acid residues with symmetry adapted perturbation theory
- Creator
- Gregory, Kasimir P.; Webber, Grant B.; Wanless, Erica J.; Page, Alister J.
- Relation
- ARC.DP190100788 http://purl.org/au-research/grants/arc/DP190100788 & FL170100032 http://purl.org/au-research/grants/arc/FL170100032
- Relation
- Electronic Structure Vol. 5, Issue 1, no. 014007
- Publisher Link
- http://dx.doi.org/10.1088/2516-1075/acbe84
- Publisher
- Institute of Physics Publishing Ltd.
- Resource Type
- journal article
- Date
- 2023
- Description
- Hofmeister effects, and more generally specific ion effects, are observed broadly in biological systems. However, there are many cases where the Hofmeister series might not be followed in complex biological systems, such as ion channels which can be highly specific to a particular ion. An understanding of how ions from the Hofmeister series interact with the proteinogenic amino acids will assist elucidation of why some binding interactions may be favoured over others. Using symmetry adapted perturbation theory (SAPT2 + 3), the interaction energies between a selection of anions and each amino acid have been investigated. The interaction strengths become more favourable in accordance with the Hofmeister series, and also with increasing polarity of the amino acids (with the exception of the negatively charged amino acid side chains). Furthermore, the interactions are generally most favourable when they simultaneously involve the side chain and both protic moieties of the backbone. The total interaction energy in these anion–amino acid complexes is also primarily determined by its electrostatic component, in a manner proportional to the þ ('sho') value of the anion.
- Subject
- hofmeister series; specific ion effects; charge density; amino acids
- Identifier
- http://hdl.handle.net/1959.13/1482510
- Identifier
- uon:50954
- Identifier
- ISSN:2516-1075
- Rights
- Original content from this work may be used under the terms of the Creative Commons Attribution 4.0 license. Any further distribution of this work must maintain attribution to the author(s) and the title of the work, journal citation and DOI. (http://creativecommons.org/licenses/by/4.0/).
- Language
- eng
- Full Text
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