Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
Author:
Affiliation:
1. Chemistry of Interfaces, Luleå University of Technology, SE-971 87, Luleå, Sweden
Funder
Engineering and Physical Sciences Research Council
Research Councils UK
Kempestiftelserna
Alzheimerfonden
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01095
Reference26 articles.
1. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
2. Propagating structure of Alzheimer's -amyloid(10-35) is parallel -sheet with residues in exact register
3. Constraints on Supramolecular Structure in Amyloid Fibrils from Two-Dimensional Solid-State NMR Spectroscopy with Uniform Isotopic Labeling
4. Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
5. Solid-State NMR Studies of Amyloid Fibril Structure
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1. Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy;Chemical Communications;2023
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3. Fine Structure in Isotopic Peak Distributions Measured Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: A Comparison between an Infinity ICR Cell and a Dynamically Harmonized ICR Cell;Journal of the American Society for Mass Spectrometry;2022-06-28
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