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Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
Protein domains without the usual distribution of amino acids, called low complexity (LC) domains, can be prone to self-assembly into amyloid-like fibrils. Self-assembly of LC domains that are nearly devoid of hydrophobic residues, such as the 214-residue LC domain of the RNA-binding protein FUS, is...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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Nature Publishing Group UK
2020
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7665218/ https://www.ncbi.nlm.nih.gov/pubmed/33184287 http://dx.doi.org/10.1038/s41467-020-19512-3 |