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EETI-II is a three-disulfide cysteine knot, while Z33 is composed of two antiparallel 3.613-helices bridged by a short loop. These two proteins were selected for several reasons. First, both EETI-II and Z33 are highly representative of small protein scaffolds that are of interest in developing novel protein functionality. EETI-II-like cysteine knots have high thermal and proteolytic stability, tolerance to mutation, oral bioavailability, and low immunogenicity, making them attractive targets for therapeutic protein engineering. Minimal helical scaffolds such as Z33 have also been extensively used to engineer novel biological functions. Since α-helix interfaces are commonplace in protein-protein binding interactions, such scaffolds are routinely evolved to bind proteins, and thus to elicit biologically relevant functions.