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Patchy proteins, anions and the Hofmeister series

Lund, Mikael LU orcid and Jungwirth, Pavel (2008) In Journal of Physics Condensed Matter 20(49).
Abstract

We investigate specific anion binding to a range of patchy protein models and use our results to probe protein-protein interactions for aqueous lysozyme solutions. Our molecular simulation studies show that the ion-protein interaction mechanism and strength largely depend on the nature of the interfacial amino acid residues. Via direct ion pairing, small anions interact with charged side-chains while larger anions are attracted to non-polar residues due to several solvent assisted mechanisms. Incorporating ion and surface specificity into a mesoscopic model for protein-protein interactions we calculate the free energy of interaction between lysozyme molecules in aqueous solutions of sodium chloride and sodium iodide. In agreement with... (More)

We investigate specific anion binding to a range of patchy protein models and use our results to probe protein-protein interactions for aqueous lysozyme solutions. Our molecular simulation studies show that the ion-protein interaction mechanism and strength largely depend on the nature of the interfacial amino acid residues. Via direct ion pairing, small anions interact with charged side-chains while larger anions are attracted to non-polar residues due to several solvent assisted mechanisms. Incorporating ion and surface specificity into a mesoscopic model for protein-protein interactions we calculate the free energy of interaction between lysozyme molecules in aqueous solutions of sodium chloride and sodium iodide. In agreement with experiment, our finding is that 'salting out' follows the reverse Hofmeister series for pH below the iso-electric point and the direct series for pH above pI.

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Please use this url to cite or link to this publication:
author
and
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physics Condensed Matter
volume
20
issue
49
article number
494218
pages
4 pages
publisher
IOP Publishing
external identifiers
  • scopus:57449107982
ISSN
0953-8984
DOI
10.1088/0953-8984/20/49/494218
language
English
LU publication?
no
id
b4c63a55-905a-43ec-80b6-3413254aa6a5
date added to LUP
2021-11-12 13:07:43
date last changed
2025-04-04 14:49:14
@article{b4c63a55-905a-43ec-80b6-3413254aa6a5,
  abstract     = {{<p>We investigate specific anion binding to a range of patchy protein models and use our results to probe protein-protein interactions for aqueous lysozyme solutions. Our molecular simulation studies show that the ion-protein interaction mechanism and strength largely depend on the nature of the interfacial amino acid residues. Via direct ion pairing, small anions interact with charged side-chains while larger anions are attracted to non-polar residues due to several solvent assisted mechanisms. Incorporating ion and surface specificity into a mesoscopic model for protein-protein interactions we calculate the free energy of interaction between lysozyme molecules in aqueous solutions of sodium chloride and sodium iodide. In agreement with experiment, our finding is that 'salting out' follows the reverse Hofmeister series for pH below the iso-electric point and the direct series for pH above pI.</p>}},
  author       = {{Lund, Mikael and Jungwirth, Pavel}},
  issn         = {{0953-8984}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{49}},
  publisher    = {{IOP Publishing}},
  series       = {{Journal of Physics Condensed Matter}},
  title        = {{Patchy proteins, anions and the Hofmeister series}},
  url          = {{http://dx.doi.org/10.1088/0953-8984/20/49/494218}},
  doi          = {{10.1088/0953-8984/20/49/494218}},
  volume       = {{20}},
  year         = {{2008}},
}