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Figure 1

From: Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth

Figure 1

Characteristics of amelogenins and Ag I/II. (a) Hydrophobicity plot of AmH; (b) Hydrophobicity plot of Ag I/II; (c) Schematic representations of Ag I/II primary and tertiary structures. Position of Ag I/II and sequence comparison between AmH (upper) and Ag I/II (down). Ag I/II of S.mutans contains 1,566 amino acids (AA): with an N-terminal signal motif, followed by an alanine repeat region (201aa to 474aa) and a proline repeat region (834aa to 991aa). The cell wall anchor domain is located at the C-terminus. AmH and Ag I/II share 19.4% identity and 24% similarity of protein sequence. Most of identical amino acids are proline; (d) Agarose gel electrophoresis (1%) of the colony PCR products showing the BL21 clones containing AmH and Ag I/II gene. M, DM2000 Marker; SDS gelatin electrophoresis showed that the molecular weight of AmH about 27 kd, Ag I/II about 34 kd.

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