Characterisation of the interactions of aromatic amino acids with diacetyl phosphatidylcholine
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2004/CP/B312184D
Reference36 articles.
1. The structure of the antimicrobial peptide Ac-RRWWRF-NH2 bound to micelles and its interactions with phospholipid bilayers
2. The Effects of Hydrophobic Mismatch between Phosphatidylcholine Bilayers and Transmembrane α-Helical Peptides Depend on the Nature of Interfacially Exposed Aromatic and Charged Residues
3. High-resolution structures and dynamics of membrane protein–lipid complexes: a critique
4. A Helix-Loop-Helix Peptide at the Upper Lip of the Active Site Cleft of Lysozyme Confers Potent Antimicrobial Activity with Membrane Permeabilization Action
5. Domain Formation in Phosphatidylcholine Bilayers Containing Transmembrane Peptides: Specific Effects of Flanking Residues
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