Characterization of oligomeric intermediate states populated at an early stage of misfolding and aggregation is essential to understanding molecular mechanism of pathogenic protein aggregation. Growing evidence also suggests that oligomeric species are more toxic than mature fibrillar counterparts. Here, we describe procedures for isolating oligomeric species of an aggregation-prone protein, transthyretin, associated with protein misfolding disorders, including cardiomyopathy and polyneuropathy....
[NMR paper] Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid-? (A?) protein aggregates. Binding of A? oligomers to membrane-anchored huPrP has been suggested to trigger neurotoxic cell signaling in Alzheimer's disease, while an N-terminal soluble fragment of huPrP can sequester A? oligomers and reduce their toxicity. Synthetic oligomeric A? species are known to be heterogeneous, dynamic and transient, rendering their structural investigation particularly...
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[NMR paper] Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Related Articles Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Magn Reson Chem. 2020 Nov 08;:
Authors: Vugmeyster L, Ostrovsky D
Abstract
We describe a new method for measuring molecular dynamics based on the deuterium solid-state nuclear magnetic resonance (NMR) quadrupolar order rotating frame relaxation rate R1?,Q under static conditions. The observed...
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[NMR paper] Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.
Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.
Related Articles Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.
J Struct Biol. 2018 Mar 28;:
Authors: Ma CW, Zhang J, Dong XQ, Lu JX
Abstract
High-order assemblies of amelogenin, the major protein in enamel protein matrix, are believed to act as the template for enamel mineral formation. The Leucine-rich amelogenin (LRAP) is a natural splice-variant of amelogenin, a functional protein...
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[NMR paper] Solid-State NMR Studies Reveal Native-like ?-sheet Structures in Transthyretin amyloid.
Solid-State NMR Studies Reveal Native-like ?-sheet Structures in Transthyretin amyloid.
Related Articles Solid-State NMR Studies Reveal Native-like ?-sheet Structures in Transthyretin amyloid.
Biochemistry. 2016 Sep 2;
Authors: Lim KH, Dasari AK, Hung IF, Gan Z, Kelly JW, Wright PE, Wemmer DE
Abstract
Structural characterization of amyloid rich in cross-? structures is crucial for unraveling molecular basis of protein misfolding and amyloid formation associated with a wide range of human disorders. Elucidation of the ?-sheet...
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Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00164/20160323/images/medium/bi-2016-00164v_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00164
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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[NMR paper] Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Biochemistry. 2016 Mar 21;
Authors: Lim KH, Dasari AK, Hung I, Gan Z, Kelly JW, Wemmer DE
Abstract
Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural...
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03-22-2016 01:46 PM
[NMR paper] Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Related Articles Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
FEBS J. 2013 Apr 20;
Authors: Renault M, García J, Cordeiro TN, Baldus M, Pons M
Abstract
Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes...
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04-23-2013 08:37 PM
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
CD and Solid-State NMR Studies of Low-Order Oligomers of Transthyretin
Linear Mode
