Model peptide studies of Ag+ binding sites from the silver resistance protein SilE
- Chabert, Valentin University of Fribourg, Department of Chemistry, Switzerland
- Hologne, M. University of Lyon, CNRS, UCB Lyon 1, ENS-Lyon, Institut des Sciences Analytiques, Villeurbanne, France
- Sénèque, O. University of Grenoble Alpes, CNRS, Grenoble, France
- Crochet, Aurélien University of Fribourg, Fribourg Center for Nanomaterials, Switzerland
- Walker, O. University of Lyon, CNRS, UCB Lyon 1, ENS-Lyon, Institut des Sciences Analytiques, Villeurbanne, France
- Fromm, Katharina M. University of Fribourg, Department of Chemistry, Switzerland
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01.06.2017
Published in:
- Chemical Communications. - 2017, vol. 53, no. 45, p. 6105–6108
English
Using model peptides, each of the nine MX2H or HXnM (n = 1, 2) motifs of the silver resistance protein SilE has been shown to coordinate to one Ag+ ion by its histidine and methionine residues with Kd in the μM range. This suggests an Ag+ buffering role for SilE in the case of high Ag+ overload.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Chimie
- Language
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- English
- Classification
- Chemistry
- License
- License undefined
- Identifiers
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- RERO DOC 288914
- DOI 10.1039/C7CC02630G
- Persistent URL
- https://folia.unifr.ch/unifr/documents/305485
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