Uses of Phage Display in Agriculture: Sequence Analysis and Comparative Modeling of Late Embryogenesis Abundant Client Proteins Suggest Protein-Nucleic Acid Binding Functionality
Figure 1
A graphic depiction of the region of the client proteins to which the SMP1 or GmPM28 proteins bound. In each graph, the full-length protein is depicted as a black bar centered at zero on the Hopp/Woods hydrophilicity plot [57] for the protein (retrieved from Expasy Protscale [35]). Recognizable motifs present in the protein are represented as red bars on the black bar under which the Pfam [58] acronym defining the motif superfamily is displayed. The region of the full-length protein displayed on the phage and captured by the LEA is shaded grey. When this region overlaps with a recognizable motif, the protein is assigned to (b) (A motif bound). When it coincides with the most, or among the most, hydrophilic of the proteins regions, it is placed in (a) (or marked by an asterisk in (b)). If the LEA-bound fragment is neither the most hydrophilic nor encoding a recognizable motif, it is placed in (c) (no recognizable attribute bound). In each graph, the size, in amino acids, of the protein moiety bound by the LEA is provided as well as the number of independently acquired clones. If the clones were of different lengths, the number of clones of a specific length is provided. Whether the clone was bound by SMP1 or GmPM28 and the temperature at which the binding occurred are also provided.
