Functional rapidly folding proteins from simplified amino acid sequences

By D. Riddle, Jed V. Santiago, Susan T. Bray-Hall, N. Doshi, V. Grantcharova, Qian Yi, David Baker. 1997

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A surprising simplicity to protein folding (2000, background): “First, large changes in amino-acid sequence, either experimenta”
The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection. (2007, background): “For example, novel folded variants of protein L and the Src SH3 domain have been identified using phagedisplay technology (Gu et al., 1995; Riddle et al., 1997), while computational protein design has allowed for the complete redesign of sequences capable of folding to naturally occurring structures”
Protein design: a perspective from simple tractable models (1998, background): “Of course, there exist clever experimental approaches, such as phage display [7], that bias experimental sequence searches towards better candidates.”