Protein repeats: structures, functions, and evolution.

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Structure and function of WD40 domain proteins (2011, background): “WD40 repeats are thought to arise through intragenic duplication and recombination events (Andrade et al., 2001), and diversify during evolution.”
High-affinity binders selected from designed ankyrin repeat protein libraries (2004, neutral): “dtd" [ ]> Repeat proteins are ubiquitous binding molecules fundamental to many biological processe”
Rational design of alpha-helical tandem repeat proteins with closed architectures (2015, methodology): “Fragment assembly—Starting backbone models for sequence design are built using a fragment assembly protocol which is based on the standard Rosetta ab initio protocol 31 with the following modifications: (1) fragment replacement moves are performed symmetrically across all repeats, guaranteeing that ”
RepeatsDB 2.0: improved annotation, classification, search and visualization of repeat protein structures (2016, background): “Proteins with tandem repeats play important functional roles (1), are abundant in nature and related to major health threats (2–6).”
Ankyrin repeat: a unique motif mediating protein-protein interactions. (2006, methodology): “To date, more than 20 classes of repeat proteins have been identified in the expanding protein sequence data bank, among which the most abundant are leucine-rich repeat (LRR)1 proteins, ankyrin repeat (AR) proteins, armadillo/ HEAT repeat proteins, and tetratricopeptide repeat proteins (1-3).”