Hydrophobicity Scales

Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Hydrophobicity scales are ranking lists for the relative hydrophobicity of amino acids that are determined from experimental approaches. There are four types of amino acid interactions inside the protein that determine their tertiary and quaternary structures: hydrophobic, electrostatic, hydrogen bonding and van der Waals interactions. Walter Kauzmann first stated that hydrophobic interactions are the most significant property of protein folding and stability. However, the hydrophobic effect alone does not represent the whole behavior of amino acids. Researchers hope better understanding of protein hydrophobicity will improve predictions of how proteins fold into their tertiary structures.