Figure 1: Open Reading Frame analysis of the cDNA for the protein 1,6 Fructose Bisphosphate Aldolase in the species Homo sapiens. Red triangles represent start codons and vertical green lines indicate stop codons. The blue box highlights the largest open reading frame. This ORF is from nucleotides x-x and codes for a protein with a molecular weight of 39,417.91 Daltons.
Figure 2: Kyte and Doolittle Hydrophobicity plot of the Homo
sapien 1,6 FBP Aldolase. There are 4 peaks on the graph
which reach a Y-axis value of 2.00 or greater, indicating portions of the
protein hydrophobic enough to reside in a phospholipid bilayer. These
points occur near positions 80, 190, 210, and 260. These data
suggests that the protein is an integral membrane protein.
Figure 3: Hopps and Woods antigenicity plot for Homo sapien 1,6 FBP Aldolase. Highly hydrophilic regions (indicated by high Y-axis values) represent possible good epitope sites. This particular plot suggests that amino acid regions around points 10, 70, 100, 140-150, and 310-330 would be good epitopes to create an antibody for.
Figure 4: Predicted secondary structure of Homo sapiens 1,6 FBP Aldolase using Chou, Fasman, and Rose analysis. Click here to compare this prediction to a Rasmol Image of Human 1,6 FBP Aldolase.
Figure 5: Multiple sequence alignment for 1,6 FBP Aldolase
from 5 different species: Drosophila
cerevisiae, and Schistosoma
mansoni. Amino acids are compared with Black boxes indicating
residues common between 2 or more species at a given position along the
polypeptide chain. To see the full amino acid sequence for a species,
click on its name.
Figure 6: Phylogenetic tree of 1,6 FBP Aldolase from Drosophila melanogaster, Homo sapiens, Mus musculus, Saccharomyces cerevisiae, and Schistosoma mansoni. MacDNAsis created this phylogenetic tree based on amino acid conservation over time between the different species. To view the complete amino acid sequence for a species, click on its name.
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