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Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
In vitro selection by using mutated GCN4-bZIP peptides for analysis of peptide-DNA interactions
H Furusawa1, T Morii, Y Okahata
1Department of Biomolecular Engineering, Tokyo Institute of Technology, Nagatsuda, Midori-ku, Yokohama, Kanagawa 226-8501, Japan.
Nucleic Acids Symposium Series
|August 9, 2003
Abstract:
In vitro selection has been used as a method to determine the optimal binding site for DNA-binding proteins. We report here in vitro selection of dsDNA sequences that bind to mutated-GCN4-bZIP peptides. The GCN4-bZIP peptide mutated from alanine to histidine on a position-14 that contacts with DNA bound to different sequence from a binding site of wild type peptide.
