Send to

Choose Destination
Science. 1989 Jan 13;243(4888):206-10.

Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo.

Author information

Abteilung Biophysikalische Chemie, Universit├Ąt 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.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center