Journal of the American Chemical Society
Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.

Residues 18-22 are a non-native loop that replaces and joins the N and C terminal regions of the standard-topology WW domain.

Circular Permutant Of The Ww Domain With Loop 1 Excised

This miniprotein construct represents a circular permutation of the Pin1 WW
domain (loop 1 excision), with some additional mutations for stability and
removal of chromophore redundancy. The structure is very similar to that of
wild-type WW Pin1, except of course for the termini and loop 1. This miniprotein
was not designed with native-like ligand-binding function in mind.

50 mM phosphate buffer, pH 6.5, with DSS standard

Brunger, Adams, Clore, Gros, Nilges and Read