Why are Kyte-Doolittle hydropathy plots useful?
Kyte-Doolittle hydropathy plots give you information about the possible structure of a protein. A hydropathy plot can indicate potential transmembrane or surface regions in proteins (Kyte, Doolittle 1982). How does a Kyte-Doolittle hydropathy plot work? Kyte-Doolittle plots were first described in a paper by Kyte and Doolittle (1982). First, each amino acid is given a hydrophobicity score between 4.6 and -4.6. A score of 4.6 is the most hydrophobic and a score of -4.6 is the most hydrophilic. Click here to see each amino acid’s score. Then a window size is set. A window size is the number of amino acids whose hydrophobicity scores will be averaged and assigned to the first amino acid in the window. The default window size is 9 amino acids. The computer program starts with the first window of amino acids and calculates the average of all the hydrophobicity scores in that window. Then the computer program moves down one amino acid and calculates the average of all the hydrophobicity scor
