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
Folding and assembly of oligomeric proteins in Escherichia coli
โ Scribed by Carolyn M. Teschke; Jonathan King
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 640 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0958-1669
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โฆ Synopsis
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 intermediates or native-like metastable species that are not in their final conformation. Methods for optimizing the yield of correctly assembled oligomers are discussed.
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