Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional
Nissley and co-workers predict protein misfolding into kinetically trapped, entangled conformations that can bypass the proteostasis network to remain soluble but less-functional for long timescales is widespread within the E. coli proteome.
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-30548-5 |
| Summary: | Nissley and co-workers predict protein misfolding into kinetically trapped, entangled conformations that can bypass the proteostasis network to remain soluble but less-functional for long timescales is widespread within the E. coli proteome. |
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| ISSN: | 2041-1723 |