Phylogenetic trees constructed from hydrophobicity values of protein sequences.
Information about conformational properties of a protein is contained in the hydrophobicity values of the amino acids in its primary sequence. We have investigated the possibility of extracting meaningful evolutionary information from the comparison of the hydrophobicity values of the corresponding amino acids in the sequences of homologous proteins. Distance matrices for six families of homologous proteins were made on the basis of the differences in hydrophobicity values of the amino acids. The phylogenetic trees constructed from such matrices were at least as good (as judged from their faithful reflection of evolutionary relationships), as trees constructed from the usual minimum mutation distance matrix.
D000595:Amino Acid Sequence; D003459:Crystallins / Q000145:classification; D003574:Cytochrome c Group / Q000145:classification; D006454:Hemoglobins / Q000145:classification; D007328:Insulin; D009211:Myoglobin / Q000145:classification; D010802:Phylogeny; D011384:Proinsulin / Q000145:classification; D011498:Protein Precursors / Q000145:classification; D011506:Proteins / Q000145:classification*
D003459:Crystallins; D003574:Cytochrome c Group; D006454:Hemoglobins; D007328:Insulin; D009211:Myoglobin; D011498:Protein Precursors; D011506:Proteins; C013737:preproinsulin; D011384:Proinsulin