Recombinant protein folding and misfolding in Escherichia coli
✍ Scribed by Baneyx, François; Mujacic, Mirna
- Book ID
- 109908311
- Publisher
- Nature Publishing Group
- Year
- 2004
- Tongue
- English
- Weight
- 480 KB
- Volume
- 22
- Category
- Article
- ISSN
- 1087-0156
- DOI
- 10.1038/nbt1029
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High levels of expression of oligomeric proteins in heterologous systems are frequently associated with misfolding and accumulation of the polypeptides in inclusion bodies. This reflects aspects of the folding and assembly pathways of oligomeric proteins, which generally proceed from either folding
Many heterologous polypeptides fail to fold into their native state when expressed in Escherichia co~i; instead, they are either degraded by the cellular proteolytic machinery or accumulate in insoluble form, typically as inclusion bodies. Misfolding is a particularly vexing problem in the expressio
## Abstract This mini‐review focuses on the processes and consequences of protein folding and misfolding. The latter process often leads to protein aggregation and precipitation with the aggregates adopting either highly ordered (amyloid fibril) or disordered (amorphous) forms. In particular, the a