Membrane-bound structure and alignment of the antimicrobial β-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR
- 1 January 2001
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 21 (3) , 191-208
- https://doi.org/10.1023/a:1012946026231
Abstract
The antimicrobial properties of the cyclic β-sheet peptide gramicidin S are attributed to its destabilizing effect on lipid membranes. Here we present the membrane-bound structure and alignment of a...Keywords
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