Article ; Online: Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance.
The journal of physical chemistry. B
2024 Volume 128, Issue 7, Page(s) 1711–1723
Abstract: Polypeptides often self-assemble to form amyloid fibrils, which contain cross-β structural motifs and are typically 5-15 nm in width and micrometers in length. In many cases, short segments of longer amyloid-forming protein or peptide sequences also form ...
Abstract | Polypeptides often self-assemble to form amyloid fibrils, which contain cross-β structural motifs and are typically 5-15 nm in width and micrometers in length. In many cases, short segments of longer amyloid-forming protein or peptide sequences also form cross-β assemblies but with distinctive ribbon-like morphologies that are characterized by a well-defined thickness (on the order of 5 nm) in one lateral dimension and a variable width (typically 10-100 nm) in the other. Here, we use a novel combination of data from solid-state nuclear magnetic resonance (ssNMR), dark-field transmission electron microscopy (TEM), atomic force microscopy (AFM), and cryogenic electron microscopy (cryoEM) to investigate the structures within amyloid ribbons formed by residues 14-23 and residues 11-25 of the Alzheimer's disease-associated amyloid-β peptide (Aβ |
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MeSH term(s) | Microscopy, Atomic Force ; Electrons ; Protein Structure, Secondary ; Nuclear Magnetic Resonance, Biomolecular/methods ; Amyloid/chemistry ; Amyloidogenic Proteins ; Amyloid beta-Peptides/chemistry |
Chemical Substances | Amyloid ; Amyloidogenic Proteins ; Amyloid beta-Peptides |
Language | English |
Publishing date | 2024-02-13 |
Publishing country | United States |
Document type | Journal Article |
ISSN | 1520-5207 |
ISSN (online) | 1520-5207 |
DOI | 10.1021/acs.jpcb.3c07867 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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