Specific ion binding to nonpolar surface patches of proteins
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18686949
DOI
10.1021/ja803274p
Knihovny.cz E-resources
- MeSH
- Potassium Chloride chemistry MeSH
- Ions chemistry MeSH
- Potassium Iodide chemistry MeSH
- Models, Molecular MeSH
- Muramidase chemistry metabolism MeSH
- Surface Properties MeSH
- Protein Binding MeSH
- Water chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Potassium Chloride MeSH
- Ions MeSH
- Potassium Iodide MeSH
- Muramidase MeSH
- Water MeSH
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.
References provided by Crossref.org
Anion-cation contrast of small molecule solvation in salt solutions
