Foldon-guided self-assembly of ultra-stable protein fibers.

ABSTRACT: A common objective in protein engineering is the enhancement of the thermodynamic properties of recombinant proteins for possible applications in nanobiotechnology. The performance of proteins can be improved by the rational design of chimeras that contain structural elements with the desired properties, thus resulting in a more effective exploitation of protein folds designed by nature. In this paper, we report the design and characterization of an ultra-stable self-refolding protein fiber, which rapidly reassembles in solution after denaturation induced by harsh chemical treatment or high temperature. This engineered protein fiber was constructed on the molecular framework of bacteriophage P22 tail needle gp26, by fusing its helical core to the foldon domain of phage T4 fibritin. Using p

SUBMITTER: Bhardwaj A 

PROVIDER: S-EPMC2525528 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature