[NMR paper] Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
J Am Chem Soc. 2017 Apr 13;:
Authors: Wang T, Jo H, DeGrado WF, Hong M
Abstract
Water is essential for protein folding and assembly of amyloid fibrils. Internal water cavities have been proposed for several amyloid fibrils, but no direct structural and dynamical data have been reported on the water...
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04-14-2017 10:27 AM
[NMR paper] Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Related Articles Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Methods Mol Biol. 2016;1345:173-83
Authors: Tuttle MD, Courtney JM, Barclay AM, Rienstra CM
Abstract
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity...
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10-12-2015 01:04 AM
[NMR paper] Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR.
Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR.
Related Articles Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR.
Biochemistry. 2014 Oct 3;
Authors: Hoop CL, Lin HK, Kar K, Hou Z, Poirier MA, Wetzel R, van der Wel PC
Abstract
In Huntington's Disease (HD), expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation....
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10-04-2014 05:16 PM
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
J Biol Chem. 2014 Apr 4;289(14):9998-10010
Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
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05-31-2014 01:57 PM
[NMR paper] Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
J Biomol NMR. 2013 Aug;56(4):359-63
Authors: Lopez del Amo JM, Schneider D, Loquet A, Lange A, Reif B
Abstract
Dynamic Nuclear Polarization solid-state NMR...
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05-23-2014 03:21 PM
[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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02-16-2013 08:00 PM
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...
WaterDistribution, Dynamics, and Interactions withAlzheimer’s ?-Amyloid Fibrils Investigated bySolid-State NMR
Linear Mode
