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. 2010 Mar 16;16:438–444.

Figure 1.

Figure 1

Predicted secondary structures of the wild type and the mutant βA3-crystallin. The following sequences were used for secondary structures prediction: wild type (Wild_type); glutamine that residues at position 85 is replaced by a glutamic acid residue (Q85E); glutamine that residues at position 180 is replaced by a glutamic acid residue (Q180E); βA3-crystallin double deamidated mutant (Q85EQ180E); or glycine residue at position 91 is removed (G91Del). The secondary structure types are designated as follows (according to DSSP program): H=alpha helix; B=residue in isolated beta-bridge; E=extended strand, participates in beta ladder; G=3-helix (3/10 helix); I=5 helix (pi helix); T=hydrogen bonded turn; S=bend; C=the rest.