Protein folding in the periplasm of Escherichia coli
✍ Scribed by Christoph Wülfing; Andreas Plückthun
- Book ID
- 110093391
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 776 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0950-382X
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📜 SIMILAR VOLUMES
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
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