Hydrophilicity Plot is a computer plot which checks the relative summed hyrophobicity or hydrophilicity of adjacent amino acid sidechains (usually within a moving window of about 6 amino acid residues) along with the the primary sequence of a polypeptide chain. Values for contribution of sidechains of each the 20 common amino acids to hydrophobicity or hydrophilicity have been developed by Hopp & Woods, and Kyte & Doolittle, and these plots are generally named after these workers. Usually, hydrophobic regions of proteins are considered likely to be in the interior of the native protein, whereas hydrophilic domains are probable to be exposed on the surface and thus possibly antigenic sites (epitopes). At best, these are crude predictions.