Ion specific protein assembly and hydrophobic surface forces

Mikael Lund; Pavel Jungwirth; Woodward Clifford

doi:10.1103/PhysRevLett.100.258105

Ion specific protein assembly and hydrophobic surface forces

Mikael Lund, Pavel Jungwirth, Woodward Clifford

Academy of Sciences of the Czech Republic

Research output: Contribution to journal › Article › peer-review

Abstract

Large anions are attracted to hydrophobic surfaces while smaller, well solvated ions are repelled. Using a combination of explicit solvent and continuum model simulations we show that this leads to significant ion-specific protein-protein interactions due to hydrophobic patches on the protein surfaces. In solutions of NaI and NaCl we calculate the potentials of mean force and find that the resulting second virial coefficients for lysozyme correspond well with experiment. We argue that ionic interactions with nonpolar surface groups may play an important role for biomolecular assembly and Hofmeister-type effects.

Original language	English
Article number	258105
Journal	Physical Review Letters
Volume	100
Issue number	25
DOIs	https://doi.org/10.1103/PhysRevLett.100.258105
Publication status	Published - 2008
Externally published	Yes

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)

Subject classification (UKÄ)

Theoretical Chemistry (including Computational Chemistry)

Access to Document

10.1103/PhysRevLett.100.258105

Cite this

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abstract = "Large anions are attracted to hydrophobic surfaces while smaller, well solvated ions are repelled. Using a combination of explicit solvent and continuum model simulations we show that this leads to significant ion-specific protein-protein interactions due to hydrophobic patches on the protein surfaces. In solutions of NaI and NaCl we calculate the potentials of mean force and find that the resulting second virial coefficients for lysozyme correspond well with experiment. We argue that ionic interactions with nonpolar surface groups may play an important role for biomolecular assembly and Hofmeister-type effects.",

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N2 - Large anions are attracted to hydrophobic surfaces while smaller, well solvated ions are repelled. Using a combination of explicit solvent and continuum model simulations we show that this leads to significant ion-specific protein-protein interactions due to hydrophobic patches on the protein surfaces. In solutions of NaI and NaCl we calculate the potentials of mean force and find that the resulting second virial coefficients for lysozyme correspond well with experiment. We argue that ionic interactions with nonpolar surface groups may play an important role for biomolecular assembly and Hofmeister-type effects.

AB - Large anions are attracted to hydrophobic surfaces while smaller, well solvated ions are repelled. Using a combination of explicit solvent and continuum model simulations we show that this leads to significant ion-specific protein-protein interactions due to hydrophobic patches on the protein surfaces. In solutions of NaI and NaCl we calculate the potentials of mean force and find that the resulting second virial coefficients for lysozyme correspond well with experiment. We argue that ionic interactions with nonpolar surface groups may play an important role for biomolecular assembly and Hofmeister-type effects.

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U2 - 10.1103/PhysRevLett.100.258105

DO - 10.1103/PhysRevLett.100.258105

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JO - Physical Review Letters

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Ion specific protein assembly and hydrophobic surface forces

Abstract

Bibliographical note

Subject classification (UKÄ)

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