[NMR paper] Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
Related Articles Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
J Am Chem Soc. 2016 Jun 10;
Authors: Williams JK, Tietze D, Lee M, Wang J, Hong M
Abstract
Together with the influenza A virus, influenza B virus causes seasonal flu epidemics. The M2 protein of influenza B (BM2) forms a tetrameric...
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06-11-2016 01:09 PM
[NMR paper] Investigation of the Curvature Induction and Membrane Localization of the Influenza Virus M2 Protein Using Static and Off-Magic-Angle Spinning Solid-State NMR of Oriented Bicelles.
Investigation of the Curvature Induction and Membrane Localization of the Influenza Virus M2 Protein Using Static and Off-Magic-Angle Spinning Solid-State NMR of Oriented Bicelles.
Investigation of the Curvature Induction and Membrane Localization of the Influenza Virus M2 Protein Using Static and Off-Magic-Angle Spinning Solid-State NMR of Oriented Bicelles.
Biochemistry. 2015 Mar 16;
Authors: Wang T, Hong M
Abstract
A wide variety of membrane proteins induce membrane curvature for function, thus it is important to develop...
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03-17-2015 05:12 PM
Solid-StateNMR Structure Determination from Diagonal-Compensated,Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints
Solid-StateNMR Structure Determination from Diagonal-Compensated,Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints
Rasmus Linser, Benjamin Bardiaux, Loren B. Andreas, Sven G. Hyberts, Vanessa K. Morris, Guido Pintacuda, Margaret Sunde, Ann H. Kwan and Gerhard Wagner
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504603g/aop/images/medium/ja-2014-04603g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504603g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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07-25-2014 06:55 PM
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR
Jonathan K. Williams, Daniel Tietze, Jun Wang, Yibing Wu, William F. DeGrado and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4041412/aop/images/medium/ja-2013-041412_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4041412
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/SJt4vbTURaE
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06-22-2013 01:40 AM
[NMR paper] Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR.
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR.
Related Articles Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR.
J Am Chem Soc. 2013 Jun 11;
Authors: Williams JK, Tietze D, Wang J, Wu Y, Degrado WF, Hong M
Abstract
The M2 protein of influenza A viruses forms a tetrameric proton channel that is targeted by the amantadine class of antiviral drugs. A S31N mutation in...
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06-14-2013 07:31 PM
[NMR paper] pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
Related Articles pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
Biophys J. 2013 Apr 16;104(8):1698-708
Authors: Williams JK, Zhang Y, Schmidt-Rohr K, Hong M
Abstract
The M2 protein of the influenza virus conducts protons into the virion under external acidic pH. The proton selectivity of...
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04-23-2013 08:37 PM
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
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10-22-2011 10:16 AM
Mechanisms of proton conduction and gating in influenza m2 proton channels from solid
Mechanisms of proton conduction and gating in influenza m2 proton channels from solid-state NMR.
Related Articles Mechanisms of proton conduction and gating in influenza m2 proton channels from solid-state NMR.
Science. 2010 Oct 22;330(6003):505-8
Authors: Hu F, Luo W, Hong M
The M2 protein of influenza viruses forms an acid-activated tetrameric proton channel. We used solid-state nuclear magnetic resonance spectroscopy to determine the structure and functional dynamics of the pH-sensing and proton-selective histidine-37 in M2 bound to a...
Solid-StateNMR Investigation of the Conformation,Proton Conduction, and Hydration of the Influenza B Virus M2 TransmembraneProton Channel
Linear Mode
