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Molecular mechanisms of ion-specific effects on proteins

Tutkimustuotosvertaisarvioitu

Standard

Molecular mechanisms of ion-specific effects on proteins. / Rembert, Kelvin B.; Paterová, Jana; Heyda, Jan; Hilty, Christian; Jungwirth, Pavel; Cremer, Paul S.

julkaisussa: Journal of the American Chemical Society, Vuosikerta 134, Nro 24, 20.06.2012, s. 10039-10046.

Tutkimustuotosvertaisarvioitu

Harvard

Rembert, KB, Paterová, J, Heyda, J, Hilty, C, Jungwirth, P & Cremer, PS 2012, 'Molecular mechanisms of ion-specific effects on proteins', Journal of the American Chemical Society, Vuosikerta. 134, Nro 24, Sivut 10039-10046. https://doi.org/10.1021/ja301297g

APA

Rembert, K. B., Paterová, J., Heyda, J., Hilty, C., Jungwirth, P., & Cremer, P. S. (2012). Molecular mechanisms of ion-specific effects on proteins. Journal of the American Chemical Society, 134(24), 10039-10046. https://doi.org/10.1021/ja301297g

Vancouver

Rembert KB, Paterová J, Heyda J, Hilty C, Jungwirth P, Cremer PS. Molecular mechanisms of ion-specific effects on proteins. Journal of the American Chemical Society. 2012 kesä 20;134(24):10039-10046. https://doi.org/10.1021/ja301297g

Author

Rembert, Kelvin B. ; Paterová, Jana ; Heyda, Jan ; Hilty, Christian ; Jungwirth, Pavel ; Cremer, Paul S. / Molecular mechanisms of ion-specific effects on proteins. Julkaisussa: Journal of the American Chemical Society. 2012 ; Vuosikerta 134, Nro 24. Sivut 10039-10046.

Bibtex - Lataa

@article{9eb54318a47d4cb78be0225fc3cbdccb,
title = "Molecular mechanisms of ion-specific effects on proteins",
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.",
author = "Rembert, {Kelvin B.} and Jana Paterov{\'a} and Jan Heyda and Christian Hilty and Pavel Jungwirth and Cremer, {Paul S.}",
year = "2012",
month = "6",
day = "20",
doi = "10.1021/ja301297g",
language = "English",
volume = "134",
pages = "10039--10046",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "24",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Molecular mechanisms of ion-specific effects on proteins

AU - Rembert, Kelvin B.

AU - Paterová, Jana

AU - Heyda, Jan

AU - Hilty, Christian

AU - Jungwirth, Pavel

AU - Cremer, Paul S.

PY - 2012/6/20

Y1 - 2012/6/20

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84862532625&partnerID=8YFLogxK

U2 - 10.1021/ja301297g

DO - 10.1021/ja301297g

M3 - Article

VL - 134

SP - 10039

EP - 10046

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 24

ER -