Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

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.

Bibliographic Details
Main Authors: Daniel A. Nissley, Yang Jiang, Fabio Trovato, Ian Sitarik, Karthik B. Narayan, Philip To, Yingzi Xia, Stephen D. Fried, Edward P. O’Brien
Format: Article
Language:English
Published: Nature Portfolio 2022-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-30548-5

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