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 analyses of the amyloidogenic intermediate and amyloid aggregates of transthyretin (TTR) using solution and solid-state NMR spectroscopy. Our solution NMR results show that one of the two main ?-sheet structures (CBEF ?-sheet) is maintained in the aggregation-competent intermediate, while the other DAGH ?-sheet is more flexible on ms time scales. Mag-ic-angle-spinning solid-state NMR revealed that AB loop regions interacting with strand A in the DAGH ?-sheet undergo conformational changes, leading to the destabilized DAGH ?-sheet.
PMID: 26998642 [PubMed - as supplied by publisher]
[NMR paper] Mechanisms of amyloid formation revealed by solution NMR.
Mechanisms of amyloid formation revealed by solution NMR.
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Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details...
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Mechanisms of amyloid formation revealed by solution NMR
Mechanisms of amyloid formation revealed by solution NMR
Publication date: Available online 26 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Theodoros K. Karamanos , Arnout P. Kalverda , Gary S. Thompson , Sheena E. Radford</br>
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details about the mechanism of...
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[NMR paper] Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
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Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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Songlin Wang and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja212190z/aop/images/medium/ja-2011-12190z_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja212190z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6EE7uthrnLg
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01-31-2012 08:34 PM
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
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J Biol Chem. 2011 Apr 20;
Authors: Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y
Co-chaperonin GroES from E. coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i. e., the...
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[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
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J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
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