Approximate way of deducing the higher order structure of a protein, based on the principle that 20-30 consistently hydrophobic residues are necessary to make a membrane-spanning a-helix. For each amino acid residue, a weighted average of the hydrophobicity of the residue and its immediate neighbours are calculated and graphically displayed as a hydropathy plot, with hydrophobic domains plotted as positive numbers. There are several formulae for the calculation, that differ in the calculation of the moving average, the window size, and the scoring system for hydrophobicity of individual residues (eg. Kyte-Doolittle, Hopp Wood, Eisenberg).
<chemistry, investigation> A graph which shows how hydrophobic each amino acid in a polypeptide is versus where it is located on the polypeptide. The hydropathy plot is used to find clusters of hydrophobic amino acids, which could indicate that the polypeptide in question is a transmembrane protein. A transmembrane protein has hydrophilic par...Found on http://www.encyclo.co.uk/local/20973
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