Amyloid fibrils have been implicated in the pathogenesis of several neurodegenerative diseases, the most prevalent example being Alzheimer's disease (AD). Despite the prevalence of AD, relatively little is known about the structure of the associated amyloid fibrils. This has motivated our studies of fibril structures, extended here to the familial Arctic mutant of A?(1-42), E22G-A?(1-42). We found E22G-A?(M0,1-42) is toxic to Escherichia coli, thus we expressed E22G-A?(1-42) fused to the...
[NMR paper] The N-Terminal Domain of Abeta(40)-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis
The N-Terminal Domain of Abeta(40)-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis
We have developed the stochastic microscopic-order-macroscopic-disorder (MOMD) approach for elucidating dynamic structures in the solid-state from ²H NMR lineshapes. In MOMD, the probe experiences an effective/collective motional mode. The latter is described by a potential, u, which represents the local spatial-restrictions, a local-motional diffusion tensor, R, and key features of local geometry. Previously we applied MOMD to the well-structured core domain of the...
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[NMR paper] Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the ?-Sheet Core.
Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the ?-Sheet Core.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--journals.plos.org-plosone-resource-img-external-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is...
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08-05-2017 11:09 PM
[NMR paper] Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
Related Articles Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
J Phys Chem B. 2017 Jul 12;:
Authors: Vugmeyster L, Ostrovsky D, Hoatson GL, Qiang W, Falconer IB
Abstract
Aromatic residues are important markers of dynamical changes in proteins' hydrophobic cores. In this work we...
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07-13-2017 12:02 PM
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Abstract
Several amyloid fibrils have cores framed by highly dynamic, intrinsically disordered, domains that can play important roles for function and toxicity. To study these domains in detail using solid-state NMR spectroscopy, site-specific resonance assignments are required. Although the rapid dynamics of these domains lead to considerable averaging of orientation-dependent NMR interactions and thereby line-narrowing, the proton...
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11-19-2016 08:35 PM
[NMR paper] High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
J Am Chem Soc. 2015 May 22;
Authors: Colvin MT, Silvers R, Frohm B, Su Y, Linse S, Griffin RG
Abstract
The presence of amyloid plaques composed of amyloid beta (A?) fibrils is a hallmark of Alzheimer's disease (AD). The A? peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted A?1-40 and A?1-42, respectively....
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05-23-2015 10:08 AM
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
J Mol Biol. 2011 Jul 13;
Authors: Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides...
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07-19-2011 07:52 PM
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100077x/aop/images/medium/bi-2010-00077x_0004.gif
Biochemistry
DOI: 10.1021/bi100077x
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10-14-2010 04:59 AM
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR.
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR.
Biochemistry. 2010 Aug 9;
Authors: van der Wel PC, Lewandowski JR, Griffin RG
Various human diseases feature the formation of amyloid aggregates, but experimental characterization of these amyloid fibrils and their oligomeric precursors has remained challenging. Experimental...
Structural characterization of E22G Abeta(1-42) fibrils via(1)H detected MAS NMR
Linear Mode
