| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797963 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 7 Pages |
Abstract
âºIn mechanically aligned lipid bilayers, the antimicrobial peptide Distinctin is absorbed on the membrane surface. âºThe topology of distinctin does not change upon variation of lipid composition. âºTwo different tilt angles were found for the two helical chains of distinctin, with chain 1 tilted by ~24 degrees, while chain 2 by ~5 degrees.
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Authors
Raffaello Verardi, Nathaniel J. Traaseth, Lei Shi, Fernando Porcelli, Luca Monfregola, Stefania De Luca, Pietro Amodeo, Gianluigi Veglia, Andrea Scaloni,