The protein folding problem has long been a preoccupation of the biological sciences. While the amino acid sequence of the protein can be determined it appears that the biological effects of the protein are determined substantially by its surface appearance and this by its fold conformation. Prediction of the fold conformation from the amino acid sequence has been described as one of the biggest unsolved problems in science [1]. During the 1980\'s a view emerged that the hydrophobic interaction dominated the fold structure that emerged and one approach has been to look at simplified models based around this perspective.