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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.
Soluble. Most enzymes are globular. The primary way globular proteins maintain their tertiary structure is called the Hydrophobic Effect. Charged, polar hydrophilic residues on the surface. Non-polar residues seclude themselves in a hydrophobic core area.Other ways of maintaining 3 0 structure Salt Bridges and Disulfide Bridges. One feature that most globular proteins share is the ability to bind certain small molecules. The site where binding occurs is the active site.The small molecules that bind are called substrates.ther ways of maintaining 3 0 structure Salt Bridges and Disulfide Bridges. One feature that most globular proteins share is the ability to bind certain small molecules. The site where binding occurs is the active site. The small molecules that bind are called substrates.