ArticleBiochemistry2009
Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 70 citations in OpenAlex.
- Side Chain Structures of the Proton-Selective Histidine and Gating Tryptophan in Influenza BM2 Reveal Both Conservation and Variation of the Proton Conduction Mechanism.Biochemistry · 2025Article
- Ion channel structure and function of the MERS coronavirus E protein.Science advances · 2025Article
- Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025Article
- Activation of the Influenza B M2 Proton Channel (BM2).Biochemistry · 2024Article
- Conformations of influenza A M2 protein in DOPC/DOPS and E. coli native lipids and proteins.Biophysical journal · 2024Article
- Activation of the influenza B M2 proton channel (BM2).bioRxiv : the preprint server for biology · 2024Article
- A comparative study of influenza A M2 protein conformations in DOPC/DOPS liposomes and in nativebioRxiv : the preprint server for biology · 2024Article
- Direct Observation of Cholesterol Dimers and Tetramers in Lipid Bilayers.The journal of physical chemistry. B · 2021Article
- Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.Journal of molecular biology · 2020Article
- Proton-Induced Conformational and Hydration Dynamics in the Influenza A M2 Channel.Journal of the American Chemical Society · 2019Article
- X-ray Crystal Structure of the Influenza A M2 Proton Channel S31N Mutant in Two Conformational States: An Open and Shut Case.Journal of the American Chemical Society · 2019Article
- Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.Journal of structural biology · 2019Article
- Determining Cholesterol Binding to Membrane Proteins by CholesterolJournal of the American Chemical Society · 2018Article
- Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes.Membranes · 2018Article
- Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers.Journal of the American Chemical Society · 2018Article
- Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.Cellular and molecular life sciences : CMLS · 2018Review
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Rapid measurement of long-range distances in proteins by multidimensionalJournal of biomolecular NMR · 2018Article
- Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR.Journal of the American Chemical Society · 2018Article
- Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Journal of molecular biology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The dynamic and structural properties of membrane proteins are intimately affected by the lipid bilayer. One property of membrane proteins is uniaxial rotational diffusion, which depends on the membrane viscosity and thickness. This rotational diffusion is readily manifested in solid-state NMR spectra as characteristic line shapes and temperature-dependent line narrowing or broadening. We show here that this whole-body uniaxial diffusion is suppressed in lipid bilayers mimicking the composition of eukaryotic cell membranes, which are rich in cholesterol and sphingomyelin. We demonstrate this membrane-induced immobilization on the transmembrane peptide of the influenza A M2 (AM2-TM) proton channel protein. At physiological temperature, AM2-TM undergoes uniaxial diffusion faster than approximately 10(5) s(-1) in DLPC, DMPC, and POPC bilayers, but the motion is slowed by 2 orders of magnitude, to <10(3) s(-1), in a cholesterol-rich virus envelope-mimetic membrane ("viral membrane"). The immobilization is manifested as near rigid-limit (2)H quadrupolar couplings and (13)C-(1)H, (15)N-(1)H, and (13)C-(15)N dipolar couplings for all labeled residues. The immobilization suppresses intermediate time scale broadening of the NMR spectra, thus allowing high-sensitivity and high-resolution spectra to be measured at physiological temperature. The conformation of the protein in the viral membrane is more homogeneous than in model PC membranes, as evidenced by the narrow (15)N lines. The immobilization of the M2 helical bundle by the membrane composition change indicates the importance of studying membrane proteins in environments as native as possible. It also suggests that eukaryote-mimetic lipid membranes may greatly facilitate structure determination of membrane proteins by solid-state NMR.
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