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Fig. 1 | BMC Biochemistry

Fig. 1

From: Design of symmetric TIM barrel proteins from first principles

Fig. 1

Depiction of the Symmetrin backbone and topology. a The backbone model used for all Symmetrin designs. Alpha helices are colored teal. Beta sheets are colored orange. Loops are colored green. The TIM barrel fold and designed four-fold symmetry are readily apparent. b Designed secondary structure topology. Helices are colored teal. Sheets are colored in two shades of orange. Lighter shades indicate residues pointing out of the page, towards the reader. Darker shades indicate residues pointing into the page, away from the reader. Cyan lines depict the beta-barrel's hydrogen bonding network. Numbers depict residues forming their respective secondary structures. The two ideal βαβ motifs chosen for this design are colored in two shades of grey. Residues shared by both βαβ motifs are colored in horizontal stripes. For clarity, only 2 of the 8 ideal βαβ motifs constituting the TIM barrel topology are colored

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