Figure 1. The Open Reading Frame (ORF) from mouse cDNA for myosin. Red arrows indicate start codons within the gene and green lines represent stop codons. The shaded black box is the largest open reading frame within the gene. This ORF spans from nucleotides 105-5921 and encodes a protein with a molecular weight of 223254.73 Daltons.
Figure 2. Kyte-Doolittle plot for mouse myosin. The X-axis numbers the amino acids in myosin, while the Y-axis indicates relative hydrophobicity. Positive numbers on the Y-axis indicate hydrophobic regions within the protein. Readings above +1.8 suggest potential transmembrane domains in the protein. The plot indicates that myosin is not a transmembrane protein because it has few regions of sufficient hydrophobicity.
Figure 3. Hopp-Woods hydrophilicity plot for mouse myosin. The X-axis labels the amino acids in myosin and the Y-axis indicates relative hydrophilicity. More hydrophilic regions have higher antigenicity and thus make better epitopes for antibodies. In myosin, amino acids beyond #1000 show the highest antigenicity and would therefore make the best epitopes. However, there are no major peaks in the plot, suggesting that no single region contains the best epitope.
Figure 4. MacDNAsis prediction of the secondary structure for mouse myosin. Legend is located above.
Figure 5. Relative similarities of myosin from five different species. Correspondence between amino acids is indicated as a percentage. Mouse and chicken myosin show the most similarity.
Figure 6. Region from myosin amino acids #101-300 in five species. Dashes indicate regions left out to maximize similarity among the species. Shaded amino acids are shared between two or more of the species. There is excellent correspondence from amino acids #101-250, but #251-300 show much less similarity among the species. Regions with higher similarity are probably more essential to the proper function of the protein.
Click below to see the complete amino acid and/or nucleotide structure for myosin in the following species:
