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Folding and stability of recombinant crystallins expressed in Escherichia coli

✍ Scribed by R. Glockshuber; E-M. Mayr; K. Berr; S. Trinkl; R. Jaenicke

Book ID
115894828
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
127 KB
Volume
55
Category
Article
ISSN
0014-4835

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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