In this chapter, we discuss a method to determine the affinity and specificity of nearly all single-point mutants for a full-length protein binder. This method combines deep sequencing, comprehensive mutagenesis, yeast surface display, and fluorescence-activated cell sorting. This approach has been used to study sequence-function relationships for protein-protein interactions. The data can be used to determine the fine conformational epitope on the protein binder.
CITATION STYLE
Medina-Cucurella, A. V., & Whitehead, T. A. (2018). Characterizing protein-protein interactions using deep sequencing coupled to yeast surface display. In Methods in Molecular Biology (Vol. 1764, pp. 101–121). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7759-8_7
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