The secondary structure of human hexokinase 1 is further elucidated in the antigenicity plot shown in Figure 4. Hydrophilic domains are positive and hydrophobic domains are negative. Since the most hydrophilic domains are the portions of the protein that extend farthest out from its center, these domains are the most likely candidates for effective epitopes. These peptide sequences would be good epitopes against which to generate monoclonal antibodies for human hexokinase 1. Antigenicity plot of the amino acid sequence of human hexokinase 1.
Positive values are hydrophilic and negative values are hydrophobic.
A prediction of the secondary structure of human hexokinase 1 is shown in Figure 5. Blue segments are alpha-helices, red segments are pleated sheets, green segments are turns, and black segments are coils. Because the amino acid sequence turns in several locations, this secondary structure prediction further suggests that human hexokinase 1 could be an integral membrane protein. Predicted secondary structure of human hexokinase 1, showing regions of structural difference. The amino acid sequences of hexokinase 1 of five different species were compared to determine homology.