Specific ion binding to nonpolar surface patches of proteins

Mikael Lund; Lubos Vrbka; Pavel Jungwirth

doi:10.1021/ja803274p

Specific ion binding to nonpolar surface patches of proteins

Mikael Lund, Lubos Vrbka, Pavel Jungwirth

Computational Chemistry

Research output: Contribution to specialist publication or newspaper › Specialist publication article › Research

Abstract

Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.

Original language	English
Pages	11582-3
Volume	130
No.	35
Specialist publication	Journal of the American Chemical Society
Publisher	The American Chemical Society (ACS)
DOIs	https://doi.org/10.1021/ja803274p
Publication status	Published - 2008

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)

Chemical Sciences

Free keywords

Ions
Ions: chemistry
Models
Molecular
Muramidase
Muramidase: chemistry
Potassium Chloride
Muramidase: metabolism
Potassium Iodide
Potassium Chloride: chemistry
Potassium Iodide: chemistry
Protein Binding
Surface Properties
Water: chemistry
Water

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10.1021/ja803274p

http://www.ncbi.nlm.nih.gov/pubmed/18686949

Cite this

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abstract = "Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.",

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AU - Lund, Mikael

AU - Vrbka, Lubos

AU - Jungwirth, Pavel

N1 - 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)

PY - 2008

Y1 - 2008

N2 - Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.

AB - Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.

KW - Ions

KW - Ions: chemistry

KW - Models

KW - Molecular

KW - Muramidase

KW - Muramidase: chemistry

KW - Potassium Chloride

KW - Muramidase: metabolism

KW - Potassium Iodide

KW - Potassium Chloride: chemistry

KW - Potassium Iodide: chemistry

KW - Protein Binding

KW - Surface Properties

KW - Water: chemistry

KW - Water

UR - https://www.scopus.com/pages/publications/51349165268

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DO - 10.1021/ja803274p

M3 - Specialist publication article

C2 - 18686949

SN - 1520-5126

VL - 130

SP - 11582

EP - 11583

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

PB - The American Chemical Society (ACS)

ER -

Specific ion binding to nonpolar surface patches of proteins

Abstract

Bibliographical note

Subject classification (UKÄ)

Free keywords

Access to Document

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