3-dimensional structure of haemoglobin, a globular protein.

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 tails) groups are bounded towards the molecule's interior whereas polar (hydrophilic heads) ones 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:

• Enzymes, by catalyzing organic reactions taking place in the organism in mild conditions and with a great specificity. Different esterases fulfill this role.
• Messengers, by transmitting messages to regulate biological processes. This function is done by hormones, i.e. insulin etc.
• Transporters of other molecules through membranes
• Stocks of amino acids.
• Regulatory roles are also performed by globular proteins rather than fibrous proteins.

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.

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