Related ArticlesSolid-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 structure in non-crystalline amyloid has, however, remained an enormous challenge. Here we report structural analyses of the ?-sheet structure in full-length transthyretin amyloid using solid-state NMR spectroscopy. Magic-angle-spinning (MAS) solid-state NMR was employed to investigate native-like ?-sheet structures in amyloid state using selective labeling schemes for more efficient solid-state NMR studies. Analyses of extensive long-range 13C-13C correlation MAS spectra obtained with selectively 13CO- and 13C?-labeled TTR reveal that the two main ?-structures in the native state, the CBEF and DAGH ?-sheets, remain intact after amyloid formation. The tertiary structural information would be of great use for examining quaternary structure of TTR amyloid.
PMID: 27589034 [PubMed - as supplied by publisher]
[NMR paper] Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
Biopolymers. 2014 Jan;101(1):13-20
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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
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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] 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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Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
Chem Commun (Camb). 2012 Nov 25;48(91):11199-201
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[NMR paper] Solid State NMR Strategy for Characterizing Native Membrane Protein Structures.
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Acc Chem Res. 2013 Mar 7;
Authors: Murray DT, Das N, Cross TA
Abstract
Unlike water soluble proteins, the structures of helicaltransmembrane proteins depend on a very complex environment. These proteins sit in the midst of dramatic electrical and chemical gradients and are often subject to variations in the lateral pressure profile, order parameters, dielectric...
Solid-State NMR Studies of Amyloid Fibril Structure.
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Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
Solid-State NMR Studies Reveal Native-like ?-sheet Structures in Transthyretin amyloid.
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