Fly lysozyme appears to have two relatively weak hydrophilic regions and two relatively weak hydrophobic regions. The largest of these hydrophobic regions is the one surrounding aa 50. Due to the hydrophobicity, this region will display good antigenicity. Therefore, one would want to sequence this region and raise antibodies against it when producing a probe against lysozyme. Next, the secondary structure of the fly lysozyme ORF was predicted using MacDNAsis.
Primary structure refers to the actual amino acid sequence that comprise a protein.
Secondary structure refers to the local spatial arrangement of the amino acids, resulting in alpha-helices or beta strands. Tertiary structure is the 3-dimensional folding of the subunit due to forces such as disulfide bonds. Finally quaternary structure refers to interaction of separate subunits to produce a whole protein. From this prediction, fly lysozyme contains four alpha helices, eight beta pleated sheets, six coiled domains, and two major turns. When compared to a RasMol image of lysozyme, this predicted structure seems relatively consistent.