High-affinity binders selected from designed ankyrin repeat protein libraries

By H. Binz, P. Amstutz, A. Kohl, M. Stumpp, C. Briand, P. Forrer, M. Grütter, A. Plückthun. Nature Biotechnology, 2004

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Emerging themes in the computational design of novel enzymes and protein–protein interfaces (2013, background): “For instance, the ankyrin domain has been studied extensively using in vitro evolution and crystallography, yielding many insights on the importance of certain positions for its stability and binding [45].”
Engineering novel binding proteins from nonimmunoglobulin domains (2005, background): “, derived from a domain of Staphylococcus aureus protein A, and DARPins from our laborator”
Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display. (2008, background): “First, the functional size of the present phage library is very large, and is expected to cover the diversity of about 1010 members present in the initial ribosome display library that was used as template.(16) Therefore, the same input library is sampled in ribosome display and phage display; howev”
Ankyrin repeat: a unique motif mediating protein-protein interactions. (2006, methodology): “4 nM, and the interactions mainly rely on the randomized positions of the design AR protein as revealed in the crystal structure of the designed AR protein -MBP complex (80).”