Extended Data Fig. 4: Sequence and structural conservation analysis of β-barrel (BBF) and TIM-barrel folds (TBF). | Nature

Extended Data Fig. 4: Sequence and structural conservation analysis of β-barrel (BBF) and TIM-barrel folds (TBF).

From: Computational design of soluble and functional membrane protein analogues

Extended Data Fig. 4

a, Cartoon depiction of example BBF design colored by sequence diversity of all designs on an individual residue level. b, Sequence diversity plotted on a per-residue level of all BBF designs. The dotted line represents the mean sequence diversity of the structure. c, Sequence logo of residue occurrence of experimentally validated and folded BBF designs highlighting residue variability at sites critical for maintaining β-barrel topology. d, Cartoon depiction of the crystal structure of TBF_24 colored by backbone RMSD per residue when compared against the target fold (left) and the design model (right), with RMSD per residue values plotted in panel e.

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