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Globular proteins are compact, spheroid-shaped molecules formed when amino acid chains wind tightly together. Their secondary structures typically combine alpha-helices and beta-sheets. This compact three-dimensional arrangement makes globular proteins water-soluble and suitable for intracellular functions like enzyme activity and cellular signaling.

Globular proteins are water-soluble because hydrophobic amino acids pack tightly into the protein's interior core, while hydrophilic amino acids cluster on the outer surface. This arrangement allows polar amino acids on the surface to interact with water molecules, enhancing solubility in the aqueous cellular environment. Understanding protein solubility is central to the role of proteins in the human body.

In globular proteins, hydrophobic amino acids are buried deep within the spheroid structure's center, away from water. Hydrophilic amino acids are positioned on the outer surface where they can interact with the aqueous environment. This strategic arrangement stabilizes the protein's compact shape and enables its biological function.

Non-covalent interactions including hydrogen bonds, Van der Waals forces, and hydrophobic interactions maintain globular protein structure. These weak interactions make globular proteins relatively unstable and vulnerable to changes in pH or temperature, affecting their ability to function properly in the body.

Globular proteins form larger structures by associating with one or more additional proteins. Hemoglobin exemplifies this, functioning as a tetramer composed of two alpha and two beta subunits. Actin monomers similarly join together to create long helical protein strands called filaments.

A protein domain is a self-contained section of a protein capable of independently folding into its three-dimensional structure. Larger globular proteins typically contain two or more distinct domains that function as separate structural and functional units while remaining part of the larger protein molecule.

Globular proteins depend on weak non-covalent interactions to maintain their three-dimensional structure. Minor pH changes disrupt these interactions, causing conformational changes that impair protein function. For example, hemoglobin only functions within a narrow pH range of 7.35 to 7.45 and loses oxygen-binding ability if pH drops below this range.