Nuclear Magnetic Resonance and Molecular DynamicsSimulation of the Interaction between Recognition Protein H7 of theNovel Influenza Virus H7N9 and Glycan Cell Surface Receptors
Nuclear Magnetic Resonance and Molecular DynamicsSimulation of the Interaction between Recognition Protein H7 of theNovel Influenza Virus H7N9 and Glycan Cell Surface Receptors
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane helix and an adjacent amphipathic helix, the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using two-dimensional (2D) magic-angle-spinning solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
nmrlearner
Journal club
0
10-07-2013 08:31 AM
[NMR paper] Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Protein Sci. 2013 Sep 10;
Authors: Liao SY, Fritzsching KJ, Hong M
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus...
nmrlearner
Journal club
0
09-12-2013 11:02 PM
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane (TM) helix and an adjacent amphipathic helix (AH), the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using 2D magic-angle-spinning (MAS) solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
nmrlearner
Journal club
0
09-10-2013 08:44 PM
[NMR paper] Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Related Articles Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Methods Enzymol. 2013;522:365-89
Authors: Goncalves J, Eilers M, South K, Opefi CA, Laissue P, Reeves PJ, Smith SO
Abstract
G protein-coupled receptors (GPCRs) represent the largest family of membrane receptors and mediate a diversity of cellular processes. These receptors have a common seven-transmembrane helix structure, yet have evolved...
nmrlearner
Journal club
0
02-05-2013 09:51 PM
[NMR paper] Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
J Am Chem Soc. 2013 Jan 29;
Authors: Arda A, Blasco P, Varon Silva D, Schubert V, André S, Bruix M, Cañada FJ, Gabius HJ, Unverzagt C, Jimenez-Barbero J
Abstract
The current surge in defining...
[NMR paper] Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)
Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Related Articles Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Biophys J. 2000 Aug;79(2):767-75
Authors: Song Z, Kovacs FA, Wang J, Denny JK, Shekar SC, Quine JR, Cross TA
The M2 protein from the influenza A virus forms a proton channel in the virion that is essential for infection. This tetrameric protein...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular
Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular modeling.
Nucleic Acids Res. 1999 Mar 1;27(5):1392-7
Authors: Cheong HK, Cheong C, Lee YS, Seong BL,...
Nuclear Magnetic Resonance and Molecular DynamicsSimulation of the Interaction between Recognition Protein H7 of theNovel Influenza Virus H7N9 and Glycan Cell Surface Receptors
Linear Mode
