Tryptophan zippers: Stable, monomeric β-hairpins

By A. Cochran, N. Skelton, M. Starovasnik. Proceedings of the National Academy of Sciences of the United States of America, 2001

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De novo protein design, a retrospective (2020, background): “Nevertheless, in the 1990s significant progress was made toward the design of peptides that form β-hairpins, including the Trp zipper peptides that displayed well-defined β-hairpin conformations stabilized by cross-strand pairs of indole rings (Cochran et al., 2001).”
Comparison of multiple Amber force fields and development of improved protein backbone parameters (2006, background): “Trpzip2 represents an exceptionally well-defined b -hairpin, 42 stabilized by cross-strand pairs of indole rings.”