Alpha-helical folding of SilE models upon Ag(His)(Met) motif formation
- Chabert, Valentin University of Fribourg, Department of Chemistry, Switzerland
- Hologne, Maggy Université de Lyon, CNRS, UCB Lyon 1, ENS-Lyon, Institut des Sciences Analytiques, UMR 5280, Villeurbanne, France
- Sénèque, Olivier Université Grenoble Alpes, CNRS, CEA, BIG/LCBM (UMR 5249), Grenoble, France
- Walker, Olivier Université de Lyon, CNRS, UCB Lyon 1, ENS-Lyon, Institut des Sciences Analytiques, UMR 5280, Villeurbanne, France
- Fromm, Katharina M. University of Fribourg, Department of Chemistry, Switzerland
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13.09.2018
Published in:
- Chemical Communications. - 2018, vol. 54, no. 74, p. 10419–10422
English
The SilE protein is suspected to have a prominent role in Ag+ detoxification of silver resistant bacteria. Using model peptides, we elucidated both qualitative and quantitative aspects of the Ag+-induced α-helical structuring role of His- and Met-rich sequences of SilE, improving our understanding of its function within the Sil system.
- 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 323334
- DOI 10.1039/C8CC03784A
- Persistent URL
- https://folia.unifr.ch/unifr/documents/307335
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