[NMR paper] Clustering of tetrameric influenza M2 peptides in lipid bilayers investigated by (19)F solid-state NMR
Clustering of tetrameric influenza M2 peptides in lipid bilayers investigated by (19)F solid-state NMR
The influenza M2 protein forms a drug-targeted tetrameric proton channel to mediate virus uncoating and carries out membrane scission to mediate virus release. While the proton channel function of M2 has been extensively studied, the mechanism by which M2 conducts membrane scission is still not well understood. Previous fluorescence and electron microscopy studies indicated that M2 tetramers concentrate at the neck of the budding virus in the host plasma membrane. However, molecular...
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[NMR paper] A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
Biophys J. 2013 Nov 19;105(10):2333-42
Authors: Kwon B, Waring AJ, Hong M
Abstract
Domain formation in bacteria-mimetic membranes...
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07-12-2014 04:28 AM
[NMR paper] Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
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Chem Phys Lipids. 2013 Sep 24;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation...
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Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Publication date: Available online 24 September 2013
Source:Chemistry and Physics of Lipids</br>
Author(s): Lei Zhang , Lishan Liu , Sergey Maltsev , Gary A. Lorigan , Carole Dabney-Smith</br>
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor...