Article
An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.
Protein science : a publication of the Protein Society - 1 Jan 2001
Zhu H, Celinski S A, Scholtz J M, Hu J C
Abstract excerpt
The leucine zipper is a dimeric coiled-coil structural motif consisting of four to six heptad repeats, designated (abcdefg)(n). In the GCN4 leucine zipper, a position 16 in the third heptad is occupied by an Asn residue whereas the other a positions are Val residues. Recently, we have constructed variants of the GCN4 leucine zipper in which the a position Val residues were replaced by Ile. The folding and...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.