Transport-RelevantProtein Conformational Dynamics and Water Dynamics on Multiple TimeScales in an Archetypal Proton Channel: Insights from Solid-StateNMR
Transport-RelevantProtein Conformational Dynamics and Water Dynamics on Multiple TimeScales in an Archetypal Proton Channel: Insights from Solid-StateNMR
[NMR paper] Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
J Am Chem Soc. 2018 Jan 05;:
Authors: Mandala V, Gelenter MD, Hong M
Abstract
The influenza M2 protein forms a tetrameric proton channel that conducts protons from the acidic endosome into the virion by shuttling...
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01-06-2018 11:17 AM
[NMR paper] Characterization of fibril dynamics on three timescales by solid-state NMR.
Characterization of fibril dynamics on three timescales by solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Characterization of fibril dynamics on three timescales by solid-state NMR.
J Biomol NMR. 2016 Aug;65(3-4):171-91
Authors: Smith AA, Testori E, Cadalbert R, Meier BH, Ernst M
Abstract
A multi-timescale analysis of the backbone dynamics of HET-s (218-289) fibrils is described based on multiple...
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12-08-2017 02:25 PM
[NMR paper] Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Related Articles Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Chem Sci. 2016 Apr 21;7(4):2666-2673
Authors: Fehér K, Timári I, Rákosi K, Szolomájer J, Illyés TZ, Bartok A, Varga Z, Panyi G, Tóth GK, Kövér KE
Abstract
Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin containing four...
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07-03-2017 02:31 AM
[NMR paper] The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR.
The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR.
Biochemistry. 2016 Aug 29;
Authors: Kwon B, Hong M
Abstract
The influenza M2 protein is the target of the amantadine family of...
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08-31-2016 02:34 PM
Characterization of fibril dynamics on three timescales by solid-state NMR
Characterization of fibril dynamics on three timescales by solid-state NMR
Abstract
A multi-timescale analysis of the backbone dynamics of HET-s (218â??289) fibrils is described based on multiple site-specific R 1 and R 1Ď? data sets and S 2 measurements via REDOR for most backbone 15N and 13Cα nuclei. 15N and 13Cα data are fitted with motions at three timescales. Slow motion is found, indicating a global fibril motion. We further investigate the effect of 13Câ??13C...
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07-16-2016 10:22 PM
Solid-StateNMR Investigation of the Conformation,Proton Conduction, and Hydration of the Influenza B Virus M2 TransmembraneProton Channel
Solid-StateNMR Investigation of the Conformation,Proton Conduction, and Hydration of the Influenza B Virus M2 TransmembraneProton Channel
Jonathan K. Williams, Daniel Tietze, Myungwoon Lee, Jun Wang and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b03142/20160623/images/medium/ja-2016-03142j_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b03142
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/CFFUWOoK8Is
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06-24-2016 12:27 AM
[NMR paper] Protein functional dynamics in multiple timescales as studied by NMR spectroscopy.
Protein functional dynamics in multiple timescales as studied by NMR spectroscopy.
Protein functional dynamics in multiple timescales as studied by NMR spectroscopy.
Adv Protein Chem Struct Biol. 2013;92:219-51
Authors: Ortega G, Pons M, Millet O
Abstract
Protein functional dynamics are defined as the atomic thermal fluctuations or the segmental motions that are essential for the function of the biomolecule. NMR is a very versatile technique that allows obtaining quantitative information from these processes at atomic resolution....
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08-21-2013 08:49 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...
Transport-RelevantProtein Conformational Dynamics and Water Dynamics on Multiple TimeScales in an Archetypal Proton Channel: Insights from Solid-StateNMR
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