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Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase

[Image: see text] The effects of sodium thiocyanate, sodium chloride, and sodium sulfate on the ribonuclease barnase were studied using differential scanning calorimetry (DSC) and NMR. Both measurements reveal specific and saturable binding at low anion concentrations (up to 250 mM), which produces...

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Autores principales: Bye, Jordan W., Baxter, Nicola J., Hounslow, Andrea M., Falconer, Robert J., Williamson, Mike P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6640789/
https://www.ncbi.nlm.nih.gov/pubmed/31457155
http://dx.doi.org/10.1021/acsomega.6b00223
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author Bye, Jordan W.
Baxter, Nicola J.
Hounslow, Andrea M.
Falconer, Robert J.
Williamson, Mike P.
author_facet Bye, Jordan W.
Baxter, Nicola J.
Hounslow, Andrea M.
Falconer, Robert J.
Williamson, Mike P.
author_sort Bye, Jordan W.
collection PubMed
description [Image: see text] The effects of sodium thiocyanate, sodium chloride, and sodium sulfate on the ribonuclease barnase were studied using differential scanning calorimetry (DSC) and NMR. Both measurements reveal specific and saturable binding at low anion concentrations (up to 250 mM), which produces localized conformational and energetic effects that are unrelated to the Hofmeister series. The binding of sulfate slows intramolecular motions, as revealed by peak broadening in (13)C heteronuclear single quantum coherence spectroscopy. None of the anions shows significant binding to hydrophobic groups. Above 250 mM, the DSC results are consistent with the expected Hofmeister effects in that the chaotropic anion thiocyanate destabilizes barnase. In this higher concentration range, the anions have approximately linear effects on protein NMR chemical shifts, with no evidence for direct interaction of the anions with the protein surface. We conclude that the effects of the anions on barnase are mediated by solvent interactions. The results are not consistent with the predictions of the preferential interaction, preferential hydration, and excluded volume models commonly used to describe Hofmeister effects. Instead, they suggest that the Hofmeister anion effects on both stability and solubility of barnase are due to the way in which the protein interacts with water molecules, and in particular with water dipoles, which are more ordered around sulfate anions and less ordered around thiocyanate anions.
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spelling pubmed-66407892019-08-27 Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase Bye, Jordan W. Baxter, Nicola J. Hounslow, Andrea M. Falconer, Robert J. Williamson, Mike P. ACS Omega [Image: see text] The effects of sodium thiocyanate, sodium chloride, and sodium sulfate on the ribonuclease barnase were studied using differential scanning calorimetry (DSC) and NMR. Both measurements reveal specific and saturable binding at low anion concentrations (up to 250 mM), which produces localized conformational and energetic effects that are unrelated to the Hofmeister series. The binding of sulfate slows intramolecular motions, as revealed by peak broadening in (13)C heteronuclear single quantum coherence spectroscopy. None of the anions shows significant binding to hydrophobic groups. Above 250 mM, the DSC results are consistent with the expected Hofmeister effects in that the chaotropic anion thiocyanate destabilizes barnase. In this higher concentration range, the anions have approximately linear effects on protein NMR chemical shifts, with no evidence for direct interaction of the anions with the protein surface. We conclude that the effects of the anions on barnase are mediated by solvent interactions. The results are not consistent with the predictions of the preferential interaction, preferential hydration, and excluded volume models commonly used to describe Hofmeister effects. Instead, they suggest that the Hofmeister anion effects on both stability and solubility of barnase are due to the way in which the protein interacts with water molecules, and in particular with water dipoles, which are more ordered around sulfate anions and less ordered around thiocyanate anions. American Chemical Society 2016-10-25 /pmc/articles/PMC6640789/ /pubmed/31457155 http://dx.doi.org/10.1021/acsomega.6b00223 Text en Copyright © 2016 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Bye, Jordan W.
Baxter, Nicola J.
Hounslow, Andrea M.
Falconer, Robert J.
Williamson, Mike P.
Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title_full Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title_fullStr Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title_full_unstemmed Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title_short Molecular Mechanism for the Hofmeister Effect Derived from NMR and DSC Measurements on Barnase
title_sort molecular mechanism for the hofmeister effect derived from nmr and dsc measurements on barnase
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6640789/
https://www.ncbi.nlm.nih.gov/pubmed/31457155
http://dx.doi.org/10.1021/acsomega.6b00223
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