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Globular proteins are folded such that their tertiary structure consists of the polar, or hydrophilic, amino acids arranged on the outside and the nonpolar, or hydrophobic, amino acids on the inside of the three-dimensional shape. This arrangement is responsible for the solubility of globular proteins in water.
The important factor for tertiary structure is that it contains only one polypeptide. If more than one is involved then it becomes quaternary structure. Tertiary protein domains are formed by combinations of disulfide bonds, hydrogen bonds, ionic bonds, and non-polar hydrophobic interactions.ertiary protein structure is one step more complicated than secondary structure. Recall that secondary structures are made of alpha helices and beta-pleated sheets. These are both local structures.