Protein misfolding and self-assembling into amyloid structures are associated with a number of diseases. Characterization of protein amyloid formation reactions is a challenging task as transient populations of multiple species are involved. Here we outline a method for identification and characterization of the individual soluble states during protein amyloid formation. The method combines NMR translational diffusion measurements with multilinear data analysis.
[NMR paper] 31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
Biochim Biophys Acta Biomembr. 2020 07 01;1862(7):183290
Authors: Haya K,...
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[NMR paper] Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Related Articles Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Biophys Rev. 2018 May 31;:
Authors: Martial B, Lefèvre T, Auger M
Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer's, Parkinson's, type II diabetes, and Creutzfeldt-Jakob's...
[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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[NMR paper] Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
PLoS One. 2013;8(9):e75018
Authors: Kang L, Janowska MK, Moriarty GM, Baum J
Abstract
Aggregation of ?-synuclein (?Syn), the primary protein component in Lewy body inclusions of patients with Parkinson's disease, arises when the normally soluble intrinsically...
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Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Alexander Kuhn, Puravankara Sreeraj, Rainer Po?ttgen, Hans-Dieter Wiemho?fer, Martin Wilkening and Paul Heitjans
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2020108/aop/images/medium/ja-2011-020108_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2020108
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[NMR paper] Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's
Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Related Articles Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Biochemistry. 2000 Nov 14;39(45):13748-59
Authors: Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH(2), called A...
Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data
Linear Mode
