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Protein-ion Interactions: Simulations of Bovine SerumAlbumin in Physiological Solutions of NaCl, KCl and LiCl
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. University of Cagliari. (CCBG ; BMC)
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. (CCBG ; BMC)
University of Cagliari.
(CCBG ; BMC)ORCID iD: 0000-0001-8696-3104
2017 (English)In: Israel Journal of Chemistry, ISSN 0021-2148, Vol. 57, 403-412 p.Article in journal (Refereed) Published
Abstract [en]

Specific interactions that depend on the nature of electrolytes are observed when proteins and other molecules are studied by potentiometric, spectroscopic and theoretical methods at high salt concentrations. More recently, it became clear that such interactions may also be observed in solutions that can be described by the Debye-Hückel theory, i.e., at physiological (0.1 mol dm−3) and lower concentrations. We carried out molecular dynamics simulations of bovine serum albumin in physiological solutions at T=300 and 350 K. Analysis of the simulations revealed some differences between LiCl solutions and those of NaCl and KCl. The binding of Li+ ions to the protein was associated with a negative free energy of interaction whereas much fewer Na+ and K+ ions were associated with the protein surface. Interestingly, unlike other proteins BSA does not show a preference to Na+ over K+. Quantum chemical calculations identified a significant contribution from polarisation to the hydration of Li+ and (to a lesser degree) Na+, which may indicate that polarisable force-fields will provide more accurate results for such systems.

Place, publisher, year, edition, pages
2017. Vol. 57, 403-412 p.
Keyword [en]
molecular dynamics ; specific ion effects; Hofmeister series
National Category
Theoretical Chemistry Biophysics Physical Chemistry
Research subject
Chemistry, Physical Chemistry
Identifiers
URN: urn:nbn:se:lnu:diva-64375DOI: 10.1002/ijch.201600119OAI: oai:DiVA.org:lnu-64375DiVA: diva2:1098608
Projects
SNIC 2015/1-226SNIC 2016/1-222
Funder
National Supercomputer Centre (NSC), Sweden, SNIC 2015/1-226National Supercomputer Centre (NSC), Sweden, SNIC 2016/1-222
Available from: 2017-05-24 Created: 2017-05-24 Last updated: 2017-05-24

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CiteExportLink to record
Permanent link

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Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
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  • Other locale
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Output format
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