Uncovering the role of the flexible C-terminal tail: A model study with Strep-tagged GFP.

ABSTRACT: Recently, it has been recognized that, much like an electric current in an electric circuit, dynamic disruptions from flexible, unstructured regions distal to the active region are transferred through the contact network to the active site and influence protein stability and/or function. As transmembrane proteins frequently possess the β-barrel structure, studies of proteins with this topology are required. The unstructured lid segments of the β-barrel GFP protein are conserved and could play a role in the backbone stabilization required for chromophore function. A study of the disordered C-terminus and the function within the lid is necessary. In this study, we entirely truncated the flexible C-terminal tail and investigated the N-terminal Strep-tagged GFP by fluorescence spectroscopy, an

SUBMITTER: Lassalle MW 

PROVIDER: S-EPMC5889473 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature