What defines the molecular shape of globular proteins, and why are they typically soluble in water?

Globular proteins are characterized by a compact, spherical molecular shape. Their three-dimensional structure is defined by intricate folding, forming domains with hydrophobic cores and hydrophilic surfaces. This unique folding is stabilized by various non-covalent interactions, including hydrogen bonds, van der Waals forces, and ionic bonds. Globular proteins are typically soluble in water due to the hydrophilic nature of their surface residues, which interact favorably with water molecules. This solubility facilitates their roles as enzymes, transporters, and signaling molecules in biological processes, as they can easily interact with aqueous environments within cells and bodily fluids.