Related Experiment Video
Updated: Jun 25, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
Published on: July 4, 2016
Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR
Erik Strandberg1, Pierre Tremouilhac, Parvesh Wadhwani
1Karlsruhe Institute of Technology, Institute of Biological Interfaces, Forschungszentrum Karlsruhe, P.O.B. 3640, 76021 Karlsruhe, Germany.
Abstract:
The skin secretions of amphibians are a rich source of antimicrobial peptides. The two antimicrobial peptides PGLa and magainin 2, isolated from the African frog Xenopus laevis, have been shown to act synergistically by permeabilizing the membranes of microorganisms. In this report, the literature on PGLa is extensively reviewed, with special focus on its synergistically enhanced activity in the presence of magainin 2. Our recent solid state (2)H NMR studies of the orientation of PGLa in lipid membranes alone and in the presence of magainin 2 are described in detail, and some new data from 3,3,3-(2)H(3)-L-alanine labeled PGLa are included in the analysis.
Related Concept Videos
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Activation and Inactivation of G Proteins
IP3/DAG Signaling Pathway
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
