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-Structure paper
Title | Cryo-EM of Helical Polymers. |
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Journal, issue, pages | Chem Rev, Vol. 122, Issue 17, Page 14055-14065, Year 2022 |
Publish date | Sep 14, 2022 |
![]() | Fengbin Wang / Ordy Gnewou / Armin Solemanifar / Vincent P Conticello / Edward H Egelman / ![]() ![]() |
PubMed Abstract | While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, ...While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited. This has mainly been due to the lack of familiarity with cryo-EM in the materials science and chemistry communities, in contrast to the fact that cryo-EM was developed as a biological technique. Nevertheless, the relatively few structures of self-assembled peptide nanotubes and ribbons solved at near-atomic resolution by cryo-EM have demonstrated that cryo-EM should be the method of choice for a structural analysis of synthetic helical filaments. In addition, cryo-EM has also demonstrated that the self-assembly of soft matter polymers has enormous potential for polymorphism, something that may be obscured by techniques such as scattering and spectroscopy. These cryo-EM structures have revealed how far we currently are from being able to predict the structure of these polymers due to their chaotic self-assembly behavior. |
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Methods | EM (helical sym.) |
Resolution | 3.4 - 3.8 Å |
Structure data | EMDB-24724, PDB-7rx4: EMDB-24725, PDB-7rx5: |
Source |
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![]() | STRUCTURAL PROTEIN / helical symmetry / peptide nanotube / self-assembly / DE NOVO PROTEIN |