ArticleStructure (London, England : 1993)2009
Gating mechanism of the influenza A M2 channel revealed by 1D and 2D IR spectroscopies.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed.
- AIM: A Mapping Program for Infrared Spectroscopy of Proteins.Journal of chemical theory and computation · 2022Article
- Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.The journal of physical chemistry letters · 2021Article
- Observation of Ultrafast Coherence Transfer and Degenerate States with Polarization-Controlled Two-Dimensional Electronic Spectroscopy.The journal of physical chemistry. B · 2020Article
- Quantitative Analysis of Multiplex H-Bonds.Journal of the American Chemical Society · 2020Article
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- Equilibrium versus Nonequilibrium Peptide Dynamics: Insights into Transient 2D IR Spectroscopy.The journal of physical chemistry. B · 2018Review
- Two-Dimensional Spectroscopy Is Being Used to Address Core Scientific Questions in Biology and Materials Science.The journal of physical chemistry. B · 2018Review
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Computing infrared spectra of proteins using the exciton model.Journal of computational chemistry · 2017Article
- GXXXG-Mediated Parallel and Antiparallel Dimerization of Transmembrane Helices and Its Inhibition by Cholesterol: Single-Pair FRET and 2D IR Studies.Angewandte Chemie (International ed. in English) · 2017Article
- Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Physical chemistry chemical physics : PCCP · 2016Article
- Spatially Resolved Two-Dimensional Infrared Spectroscopy via Wide-Field Microscopy.ACS photonics · 2016Article
- Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.Methods in molecular biology (Clifton, N.J.) · 2016Article
- How Sensitive is the Amide I Vibration of the Polypeptide Backbone to Electric Fields?Chemphyschem : a European journal of chemical physics and physical chemistry · 2015Article
- Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductance.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Probing Site-Specific Structural Information of Peptides at Model Membrane Interface In Situ.Journal of the American Chemical Society · 2015Article
- Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- Catching protein structural dynamics by two-dimensional infrared spectroscopy.Biophysical journal · 2015Article
- Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.Chemical science · 2015Article
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7 authors.
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Abstract
The pH-controlled M2 protein from influenza A is a critical component of the virus and serves as a target for the aminoadamantane antiflu agents that block its H+ channel activity. To better understand its H+ gating mechanism, we investigated M2 in lipid bilayers with a new combination of IR spectroscopies and theory. Linear Fourier transform infrared (FTIR) spectroscopy was used to measure the precise orientation of the backbone carbonyl groups, and 2D infrared (IR) spectroscopy was used to identify channel-lining residues. At low pH (open state), our results match previously published solid-state NMR and X-ray structures remarkably well. However, at neutral pH when the channel is closed, our measurements indicate that a large conformational change occurs that is consistent with the transmembrane alpha-helices rotating by one amino acid register--a structural rearrangement not previously observed. The combination of simulations and isotope-labeled FTIR and 2D IR spectroscopies provides a noninvasive means of interrogating the structures of membrane proteins in general and ion channels in particular.
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