Related ArticlesCharacterization 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 site-specific R 1 and R 1? data sets and S (2) measurements via REDOR for most backbone (15)N and (13)C? nuclei. (15)N and (13)C? data are fitted with motions at three timescales. Slow motion is found, indicating a global fibril motion. We further investigate the effect of (13)C-(13)C transfer in measurement of (13)C? R 1. Finally, we show that it is necessary to go beyond the Redfield approximation for slow motions in order to obtain accurate numerical values for R 1?.
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 sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Related Articles Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Biomol NMR Assign. 2016 May 10;
Authors: Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH
Abstract
The formation of fibrils of the amyloid-? (A?) peptide is considered to be a key event in the pathology of Alzheimer's disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular...
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05-12-2016 09:30 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
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2
Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2
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 this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the...
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11-17-2014 12:39 AM
[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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04-22-2014 03:54 PM
[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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09-21-2013 06:50 PM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
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01-12-2011 11:11 AM
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
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/uAjKy7vWoHs
Characterization of fibril dynamics on three timescales by solid-state NMR.
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