Abstract
Abstract Magainin 2 is a 23‐residue peptide that forms an amphipathic α ‐helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One‐ and two‐dimensional solid‐state 15 N NMR spectra of specifically 15 N‐labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is α ‐helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.
Keywords
MagaininMembranePeptideBiophysicsChemistryNuclear magnetic resonance spectroscopyLysisLipid bilayerSolid-state nuclear magnetic resonanceBilayerCell membraneProtein secondary structureNuclear magnetic resonanceAntimicrobial peptidesBiochemistryBiologyStereochemistryPhysics
Affiliated Institutions
Related Publications
The Fluid Mosaic Model of the Structure of Cell Membranes
A fluid mosaic model is presented for the gross organization and structure of the proteins and lipids of biological membranes. The model is consistent with the restrictions impo...
Structure and Dynamics of the Homologous Series of Alanine Peptides: A Joint Molecular Dynamics/NMR Study
The phi,psi backbone angle distribution of small homopolymeric model peptides is investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study. Combinin...
Optimized Molecular Dynamics Force Fields Applied to the Helix−Coil Transition of Polypeptides
Obtaining the correct balance of secondary structure propensities is a central priority in protein force-field development. Given that current force fields differ significantly ...
Molecular Dynamics Simulations of Membranes Composed of Glycolipids and Phospholipids
Lipid membranes composed of 1,2-di-(9Z,12Z,15Z)-octadecatrienoyl-3-O-β-D-galactosyl-sn-glycerol or monogalactosyldiacylglycerol (MGDG) and 1,2-dimyristoyl-sn-glycero-3-phosphoch...
<i>De Novo</i> Determination of the Crystal Structure of a Large Drug Molecule by Crystal Structure Prediction-Based Powder NMR Crystallography
The crystal structure of form 4 of the drug 4-[4-(2-adamantylcarbamoyl)-5-tert-butyl-pyrazol-1-yl]benzoic acid is determined using a protocol for NMR powder crystallography at n...
Publication Info
- Year
- 1993
- Type
- article
- Volume
- 2
- Issue
- 12
- Pages
- 2077-2084
- Citations
- 347
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
347
OpenAlex
Cite This
Burkhard Bechinger,
Michael Zasloff,
Stanley J. Opella
(1993).
Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy.
Protein Science
, 2
(12)
, 2077-2084.
https://doi.org/10.1002/pro.5560021208
Identifiers
- DOI
- 10.1002/pro.5560021208