Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel
- 10 September 2007
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1768 (12) , 3162-3170
- https://doi.org/10.1016/j.bbamem.2007.08.025
Abstract
No abstract availableKeywords
This publication has 84 references indexed in Scilit:
- Structural biology of transmembrane domains: Efficient production and characterization of transmembrane peptides by NMRProtein Science, 2007
- The Chemical and Dynamical Influence of the Anti-Viral Drug Amantadine on the M2 Proton Channel Transmembrane DomainBiophysical Journal, 2007
- Structural Similarity of a Membrane Protein in Micelles and MembranesJournal of the American Chemical Society, 2007
- Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane-Anchored Electron-Carrier Protein, Cytochrome b5Journal of the American Chemical Society, 2007
- NMR of membrane proteins in micelles and bilayers: The FXYD family proteinsMethods, 2007
- Uniformly Aligned Full-Length Membrane Proteins in Liquid Crystalline Bilayers for Structural CharacterizationJournal of the American Chemical Society, 2007
- Structure, Topology, and Tilt of Cell-Signaling Peptides Containing Nuclear Localization Sequences in Membrane Bilayers Determined by Solid-State NMR and Molecular Dynamics Simulation StudiesBiochemistry, 2007
- High-Resolution NMR Spectroscopy of a GPCR in Aligned BicellesJournal of the American Chemical Society, 2006
- Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivityProceedings of the National Academy of Sciences, 2006
- Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + ChannelScience, 2005