Related ArticlesInsights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR.
Biophys J. 2014 Aug 19;107(4):941-946
Authors: Barbet-Massin E, Felletti M, Schneider R, Jehle S, Communie G, Martinez N, Jensen MR, Ruigrok RW, Emsley L, Lesage A, Blackledge M, Pintacuda G
Abstract
(1)H-detected solid-state nuclear magnetic resonance (NMR) experiments are recorded on both intact and trypsin-cleaved sedimented measles virus (MeV) nucleocapsids under ultra-fast magic-angle spinning. High-resolution (1)H,(15)N-fingerprints allow probing the degree of molecular order and flexibility of individual capsid proteins, providing an exciting atomic-scale complement to electro microscopy (EM) studies of the same systems.
PMID: 25140429 [PubMed - as supplied by publisher]
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...
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[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...
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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...
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09-10-2013 08:44 PM
[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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03-27-2013 03:33 PM
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
Chemphyschem. 2011 Apr 4;12(5):915-8
Authors: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH
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03-29-2011 07:04 PM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
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02-24-2011 11:04 AM
[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...
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11-19-2010 08:29 PM
[NMR paper] Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Related Articles Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Biophys Chem. 1997 Oct;68(1-3):233-41
Authors: Auger M
The purpose of the present study is the investigation of the structure and dynamics of biological membranes using solid-state nuclear magnetic resonance (NMR) spectroscopy. Two approaches are used in our laboratory. The first involves the measurement of high-resolution 13C and 1H spectra obtained by the magic angle spinning...
Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR.
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