Lopez del Amo, J.-M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-? peptide: perspectives for DNP. J. Biomol. NMR, 2013: p. 1-5.
Dynamic Nuclear Polarization solid-state NMR holds the potential to enable a dramatic increase in sensitivity by exploiting the large magnetic moment of the electron. However, applications to biological solids are hampered in uniformly isotopically enriched biomacromolecules due to line broadening which yields a limited spectral resolution at cryogenic temperatures. We show here that high magnetic fields allow to overcome the broadening of resonance lines often experienced at liquid nitrogen temperatures. For a fibril sample of the Alzheimer's disease beta-amyloid peptide, we find similar line widths at low temperature and at room temperature. The presented results open new perspectives for structural investigations in the solid-state.
[NMR paper] Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Acc Chem Res. 2013 May 10;
Authors: Tang M, Comellas G, Rienstra CM
Abstract
Solid-state NMR (SSNMR) spectroscopy has become an important technique for studying the biophysics and structure biology of proteins. This technique is especially useful for insoluble membrane proteins and amyloid fibrils, which are essential for...
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[NMR paper] Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
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 Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
J Pept Sci. 2012 Nov;18(11):691-5
Authors: Sun N, Hartmann R, Lecher J, Stoldt M, Funke SA, Gremer L, Ludwig HH, Demuth HU, Kleinschmidt M,...
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[NMR paper] Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
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 Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Oct 8;51(41):10289-92
Authors: Antzutkin ON, Iuga D, Filippov AV, Kelly RT, Becker-Baldus J, Brown SP, Dupree R
PMID: 22976560
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Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Bioorg Med Chem. 2011 Aug 27;
Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K
Abstract
Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...
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09-20-2011 03:10 PM
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Jonathan J. Helmus, Krystyna Surewicz, Marcin I. Apostol, Witold K. Surewicz and Christopher P. Jaroniec
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206469q/aop/images/medium/ja-2011-06469q_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206469q
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/e9F1wuu5168
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Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
J Am Chem Soc. 2010 Oct 6;132(39):13765-75
Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...
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01-21-2011 12:00 PM
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
J Mol Biol. 2010 Nov 18;
Authors: Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A
Despite its importance in the context of conformational diseases, structural information is still sparse for protein fibrils. Hydrogen/deuterium exchange measurements of backbone amides allow to identify hydrogen-bonding patterns and reveal pertinent information about...
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11-26-2010 05:32 PM
[NMR paper] Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's
Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Related Articles Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Biochemistry. 2000 Nov 14;39(45):13748-59
Authors: Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH(2), called A...