𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Formation of Soluble Recombinant Proteins in Escherichia Coli is Favored by Lower Growth Temperature

✍ Scribed by Schein, Catherine H. ;Noteborn, Mathieu H. M.

Book ID
109902225
Publisher
Nature Publishing Group
Year
1988
Tongue
English
Weight
685 KB
Volume
6
Category
Article
ISSN
1087-0156

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Yield, solubility and conformational qua
Yield, solubility and conformational quality of soluble proteins are not simultaneously favored in recombinant Escherichia coli
✍ MΓ³nica MartΓ­nez-Alonso; Elena GarcΓ­a-FruitΓ³s; Antonio Villaverde πŸ“‚ Article πŸ“… 2008 πŸ› John Wiley and Sons 🌐 English βš– 235 KB

## Abstract Many enzymes or fluorescent proteins produced in __Escherichia coli__ are enzymatically active or fluorescent respectively when deposited as inclusion bodies. The occurrence of insoluble but functional protein species with native‐like secondary structure indicates that solubility and co

Plasmid maintenance in Escherichia coli
Plasmid maintenance in Escherichia coli recombinant cultures is dramatically, steadily, and specifically influenced by features of the encoded proteins
✍ JosΓ© L. Corchero; Antonio Villaverde πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 120 KB

A set of eight closely related plasmid constructs carrying CI857-controlled recombinant genes has been used as a model to study plasmid stability in Escherichia coli, in the absence of antibiotic selection. Plas- mid loss rates and relative interdivision times of plasmidbearing cells and plasmid-fre