Article
Structural rearrangements and the unfolding mechanism of a Trigger Factor mutant studied by multiple structural probes.
Biochimica et biophysica acta - 1 Jun 2009
Fan Dong-Jie, Ding Yan-Wei, Zhou Jun-Mei
Abstract excerpt
Trigger Factor (TF) is a three-domain chaperone which catalyzes nascent peptide folding and harbors peptidyl-prolyl cis-trans isomerase activity. The multi-domain structure of TF makes it an interesting and challenging candidate for studies of the structural properties and functional behavior of individual domains or combined domain constructs. Here we constructed a TF mutant, NC, combining the N- and C-domains...
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