Globular proteins, or spheroproteins are one of the two main protein classes, comprising "globe"-like proteins that are more or less soluble in aqueous solutions (where they form colloidal solutions). This main characteristic helps distinguishing them from fibrous proteins (the other class), which are practically insoluble.
Globular structure and solubility
The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive
structural motif vocabulary. The globular nature of these proteins can be determined without the means of modern techniques, but only by using
ultracentrifuges or dynamic light
scattering techniques.
The spherical structure is induced by the protein's tertiary structure. The molecule's apolar (hydrophobic) amino acids are bounded towards the molecule's interior whereas polar (hydrophilic) amino acids are bound outwards, allowing dipole-dipole interactions with the solvent, which explains the molecule's solubility.
A wide range of roles in the organism
Unlike fibrous proteins which only play a structural function, globular proteins can act as:
Members
Among the most known globular proteins is
Hemoglobin, a member of the
globin protein family. Other globular proteins are the
immunoglobulins (IgA, IgD, IgE, IgG and IgM), and
alpha,
beta and
gamma globulins. See
protein electrophoresis for more information on the different globulins. Nearly all enzymes with major
metabolic functions are globular in shape, as well as many
signal transduction proteins.