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Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells

Biochimica et Biophysica Acta (BBA) - Biomembranes · 1999 · Vol. 1462(1-2) · pp. 71–87
Margitta DatheTorsten Wieprecht
Antimicrobial Peptides and ActivitiesProtein Hydrolysis and Bioactive PeptidesBiochemical and Structural CharacterizationAntimicrobial peptidesPeptideMembraneMelittinCathelicidinChemistryPeptide sequenceAmino acidAmphiphileBiochemistry

MeSH terms

Amino Acid SequenceAnimalsAnti-Bacterial AgentsBacteriaCell MembraneErythrocyte MembraneLipid BilayersMelittenMembrane LipidsMolecular Sequence DataPeptidesPermeabilityStructure-Activity RelationshipProtein Structure, SecondaryAntimicrobial Cationic Peptides
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References
Experimentally determined hydrophobicity scale for proteins at membrane interfaces
Nature Structural & Molecular Biology · 1996 · 1,655 citations
Amphipathic helix motif: Classes and properties
Proteins Structure Function and Bioinformatics · 1990 · 640 citations
Empirical Predictions of Protein Conformation
Annual Review of Biochemistry · 1978 · 3,142 citations
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