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J Am Chem Soc. 2012 Jun 20;134(24):10039-46. doi: 10.1021/ja301297g. Epub 2012 Jun 11.

Molecular mechanisms of ion-specific effects on proteins.

Author information

1
Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.

Abstract

The specific binding sites of Hofmeister ions with an uncharged 600-residue elastin-like polypeptide, (VPGVG)(120), were elucidated using a combination of NMR and thermodynamic measurements along with molecular dynamics simulations. It was found that the large soft anions such as SCN(-) and I(-) interact with the polypeptide backbone via a hybrid binding site that consists of the amide nitrogen and the adjacent α-carbon. The hydrocarbon groups at these sites bear a slight positive charge, which enhances anion binding without disrupting specific hydrogen bonds to water molecules. The hydrophobic side chains do not contribute significantly to anion binding or the corresponding salting-in behavior of the biopolymer. Cl(-) binds far more weakly to the amide nitrogen/α-carbon binding site, while SO(4)(2-) is repelled from both the backbone and hydrophobic side chains of the polypeptide. The Na(+) counterions are also repelled from the polypeptide. The identification of these molecular-level binding sites provides new insights into the mechanism of peptide-anion interactions.

PMID:
22687192
DOI:
10.1021/ja301297g
[Indexed for MEDLINE]

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