Characterizing the binding of the GCN4 leucine zipper domain to DNA sequences

GCN4 is a well-known transcription factor from S. cerevisiae, and its leucine zipper domain comprises a coiled-coil forming region and a DNA-binding basic region. In the framework of the iSenseDNA European project, this model peptide will be used to test the ability of tailor-made supercoiled DNA constructs to sense protein conformation, by virtue of its very clear disorder to order transition happening in its basic region upon DNA binding. We propose to employ SAXS-WAXS (and eventually their time-resolved variant) on ID09 to perform and in-depth characterization of the binding process, in order to validate the working hypothesis of the project and to obtain further insight on the engineering of the DNA constructs.