title: Generating random circular permutation libraries.
abstract: Protein engineering by random circular permutation is an effective tool for tailoring protein topology with potential functional benefits including improved catalytic activity. This method involves covalently connecting the native protein termini with a peptide linker and cleaving a peptide bond elsewhere in the polypeptide sequence. Termini relocation can impact protein ternary and quaternary structure and translate into functional enhancements due to changes in protein conformation and flexibility. As the effects of new termini in specific protein locations are difficult to predict, the preparation of a library constituting all possible permutation sites is an effective search strategy for identifying variants with novel properties.
authors: Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, GA, USA, sal2@emory.edu.
authors: Stefan
authors: S
authors: Lutz
authors: Ashley B
authors: AB
authors: Daugherty
authors: Ying
authors: Y
authors: Yu
authors: Zhen
authors: Z
authors: Qian
mesh_terms: D015723:Gene Library; D015202:Protein Engineering