[NMR paper] Fibrils Emerging from Droplets: Molecular Guiding Principles behind Phase Transitions of a Short Peptide-Based Condensate Studied by Solid-State NMR
Biochemical reactions occurring in highly crowded cellular environments require different means of control to ensure productivity and specificity. Compartmentalization of reagents by liquid-liquid phase separation is one of these means. However, extremely high local protein concentrations of up to 400 mg/ml can result in pathological aggregation into fibrillar amyloid structures, a phenomenon that has been linked to various neurodegenerative diseases. Despite its relevance, the process of...
[ASAP] Binding Sites of a Position Emission Tomography Imaging Agent in Alzheimers Amyloid Fibrils Studied Using 19F Solid-State NMR
Binding Sites of a Position Emission Tomography Imaging Agent in Alzheimers Amyloid Fibrils Studied Using 19F Solid-State NMR
Pu Duan, Kelly J. Chen, Gayani Wijegunawardena, Aurelio J. Dregni, Harrison K. Wang, Haifan Wu, and Mei Hong
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c12056/20220111/images/medium/ja1c12056_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c12056
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[NMR paper] Helix Fraying and Lipid-Dependent Structure of a Short Amphipathic Membrane-Bound Peptide Revealed by Solid-State NMR.
Helix Fraying and Lipid-Dependent Structure of a Short Amphipathic Membrane-Bound Peptide Revealed by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Helix Fraying and Lipid-Dependent Structure of a Short Amphipathic Membrane-Bound Peptide Revealed by Solid-State NMR.
J Phys Chem B. 2018 06 14;122(23):6236-6250
Authors: Strandberg E, Grau-Campistany A, Wadhwani P, Bürck J, Rabanal F, Ulrich AS
Abstract
The amphipathic ?-helical...
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[NMR paper] Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Trends Biochem Sci. 2017 Oct;42(10):777-787
Authors: Meier BH, Riek R, Böckmann A
Abstract
Amyloid structures at atomic resolution have remained elusive mainly because of their extensive polymorphism and because their polymeric properties have hampered...
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[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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Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez Del Amo, J.M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP. J Biomol NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
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Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez del Amo, J.-M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-? peptide: perspectives for DNP. J. Biomol. NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
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07-19-2013 09:20 PM
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
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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Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Biomacromolecules. 2011 May 9;12(5):1546-55
Authors: Sharpe S, Simonetti K, Yau J, Walsh P
Abstract
The characterization of the molecular structure and physical properties of self-assembling peptides is an...
Fibrils Emerging from Droplets: Molecular Guiding Principles behind Phase Transitions of a Short Peptide-Based Condensate Studied by Solid-State NMR
Linear Mode
