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Science 13 January 1989:
Vol. 243. no. 4888, pp. 206 - 210
DOI: 10.1126/science.2643160
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Articles
Science, Vol 243, Issue 4888, 206-210
Copyright © 1989 by American Association for the Advancement of Science
Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
K Luger,
U Hommel,
M Herold,
J Hofsteenge,
and
K Kirschner
Abteilung Biophysikalische Chemie, Universitat Basel, Switzerland.
An important question in protein folding is whether the natural amino and carboxyl termini and the given order of secondary structure segments are critical to the stability and to the folding pathway of proteins. Here it is shown that two circularly permuted versions of the gene of a single-domain beta alpha barrel enzyme can be expressed in Escherichia coli. The variants are enzymically active and are practically indistinguishable from the original enzyme by several structural and spectroscopic criteria, despite the creation of new termini and the cleavage of a surface loop. This novel genetic approach should be useful for protein folding studies both in vitro and in vivo.
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