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. Author manuscript; available in PMC: 2018 Feb 20.
Published in final edited form as: Biochemistry. 2017 Oct 17;56(43):5720–5725. doi: 10.1021/acs.biochem.7b00722

Figure 1.

Figure 1

Ecballium elaterium trypsin inhibitor II (EETI-II) variants explored in the design and folding of heterochiral proteins. Ramachandran plots, solution nuclear magnetic resonance structure ensembles, and primary sequences with disulfide connectivity (yellow) for (A) wild-type EETI-II (Protein Data Bank entry 2IT7), (B) integrin binding EETI-II 2.5F, and (C) a heterochiral EETI-II 2.5F analogue in which the chirality of the amino acids in the protein loop is inverted relative to the chirality of the rest of the scaffold. Uppercase letters denote l-amino acids or achiral amino acids, and lowercase and underlined letters denote d-amino acids; β denotes β-alanine.