In our recent publication (Smith et al., J Biomol NMR 65:171â??191, 2016) on the dynamics of HET-s(218â??289), we reported on page 176, that calculation of solid-state NMR R1Ï? rate constants using analytical equations based on Redfield theory (Kurbanov et al., J Chem Phys 135:184104:184101â??184109, 2011) failed when the correlation time of motion becomes too long.
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
Venkata S. Mandala, Martin D. Gelenter and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b12464/20180122/images/medium/ja-2017-12464m_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b12464
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http://feeds.feedburner.com/~r/acs/jacsat/~4/ctiYCDGHbFI
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[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
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 1Ï? 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
[NMR paper] Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.
J Biomol NMR. 2014 Nov 16;
Authors: Gattin Z, Schneider R, Laukat Y, Giller K, Maier E, Zweckstetter M, Griesinger C, Benz R, Becker S, Lange A
Abstract
The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In...
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11-17-2014 12:48 PM
[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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[NMR paper] Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Related Articles Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
J Biomol NMR. 2013 Sep 19;
Authors: Zinkevich T, Chevelkov V, Reif B, Saalwächter K, Krushelnitsky A
Abstract
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NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
Lucia Banci, Ivano Bertini, Olga Blaževitš, Francesca Cantini, Moreno Lelli, Claudio Luchinat, Jiafei Mao and Miguela Vieru
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1069689/aop/images/medium/ja-2010-069689_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1069689
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http://feeds.feedburner.com/~r/acs/jacsat/~4/uAjKy7vWoHs