Examples Of Globular Proteins – Globular proteins are one of the common protein types, with water-soluble and shaped roughly like a globe or a sphere when coiled up into its functional form. Globular proteins are proteins that consist of long chains of amino acids folded up into complex shapes. In a globular protein, the amino acid chain twists and folds in a manner that enhances the protein’s solubility in water by placing polar groups of atoms at the protein’s surface.
Examples Of Globular Proteins – The primary structure of globular proteins consists of a polypeptide, or chain of amino acids joined via peptide bonds. Hydrogen bonds between carboxyl and amine groups of the amino acids contribute to the secondary structure, which in globular proteins may include alpha-helices, beta-sheets, or both. Globular proteins are only marginally stable because the free energy released when the protein folded into its native conformation is relatively small. This is because protein folding requires entropic cost.
Globular Protein Examples – Globular proteins also function as anti-bodies in the body’s immune system and as transport vehicles for other molecules in circulating blood, and they are heavily involved in the replication and repair of DNA. Globular proteins have roles in metabolic reactions; Enzymes ( catalyse metabolic reactions ), Haemoglobin ( binds to oxygen to transport it around body ), Messengers, by transmitting messages to regulate biological processes. This function is done by hormones, i.e. insulin etc. Regulatory roles are also performed by globular proteins rather than fibrous proteins. Stocks of amino acids, Transporters of other molecules through membranes.
Globular Protein Examples – Some examples of Globular proteins; Alpha globulin, Beta globulin, C3-convertase, Cadherin, Carboxypeptidase, C-reactive protein, Albumins, Ependymin, Fibrin, Gamma globulin, Hemoglobin, IgE, IgG, IgM, Integrin, Myoglobin, NCAM, Protein C, Protein S, Protein Z, Protein Z-related protease inhibitor, Serum albumin, Serum Am.
The tertiary structure of globular proteins reflects their interaction with their aqueous solvent. At a simple level, a globular protein may be considered to consist of a hydrophobic core surrounded by a hydrophilic external surface which interacts with water. The tertiary fold of the polypeptide is such that those residues with apolar side chains are buried in the centre, while the polar residues remain exposed.