Proteins play a very important role in our

bodies, from catalysing reactions to strengthening structures. And they each have specific components which differentiate them.

Proteins contain the elements carbon, hydrogen and oxygen, always nitrogen and sometimes sulfur. The building blocks of proteins are called amino acids. These are small molecules that are composed of an amine group (-NH2 ), a carboxyl group (-COOH), a hydrogen (-H) and a residual group (-R), all bonded around a single carbon atom. The residual group is the variable between all the different amino acids.

Amino acids can combine together to create a polypeptide chain. When this happens the carbon and nitrogen in the carboxyl and amine groups will bond. However, in order for this to happen they must expel the hydroxyl group and a hydrogen atom from the amine, therefore water is created. This creates a peptide bond, via a condensation reaction.

Protein structure is analysed on 4 different levels. The first of which is the primary structure. This refers to the sequence, order or type of amino acids in a polypeptide chain, that will eventually be a protein. The code for the primary structure is contained in gene(s) that code for a specific protein. The R- groups will then often determine the 3-D shape of the protein when it folds, hence it is imperative that the gene code isnt faulty.

The first level of 3-D twisting is the secondary structure of a protein. When combinations of amino acids join together the tend to fold into a particular shape. These shapes form in an attempt to achieve the most stable arrangement of hydrogen bonds between the molecules. These patterns can be different on different locations of the polypeptide chain. The two main types of secondary structure in proteins are: the -helix, a spiral, which is the most common type of secondary structure. This is where residues in the spiral twist on their axis. the - pleated sheet, a flat structure that consists of 2 or more amino acid chains , running parallel to each other, linked by hydrogen bonds. This secondary structure depends on the amino acid sequence. There are two types of complete proteins we need to know: Fibrous proteins: these contain polypeptides that combine to form tough, long fibres, that are insoluble in water. And often are majorly arranged in sheets. An example is collagen. Globular proteins: these are often individual polypeptides with complex and important tertiary structures. Theyre spherical and water soluble. An example would be enzymes.

The tertiary structure is the final 3-D shape of a polypeptide chain and is produced due to : (i) the sequence of amino acids that produces the two type of shapes and bend at certain points. (ii) the hydrophobic nature of many amino acid side chains, which will mean they must point inwards to avoid contact with water. The tertiary structure is maintained by attractive forces between the molecules in a chain e.g. Disulfide bridges, hydrogen bonds, in general ionic, covalent and intermolecular bonds form in order to provide strength.

Many proteins consist of more than one polypeptide chain and also have non-protein prosthetic groups, often vital for function. The quarternary structure refers to the conformation created when all sub-units combine to give the final protein.