Journal article

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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
  • English
Classification
Chemistry
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/305485
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