Alpha-helical folding of SilE models upon Ag(His)(Met) motif formation. Issue 74 (22nd August 2018)

• Record Type: Journal Article
• Authors: Chabert, Valentin; Hologne, Maggy; Sénèque, Olivier; Walker, Olivier; Fromm, Katharina M.
• Is Part Of: Chemical communications. Volume 54:Issue 74(2018)
• Page Start: 10419
• Page End: 10422
• Publication Date: 2018-08-22
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c8cc03784a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : The first structures and silver binding affinities of SilE key sequences provide insights in the functioning of the Sil system. Abstract : 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.