How the Structure of Proteins Are Related to Their Function

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Proteins are polymers of amino acids joined by strong peptide bonds. The combination of any of the twenty amino acids in any length and sequence allows an almost infinite number of possible structures and functions. This essay will detail how the structure of proteins are related to their function. The sequence of amino acids in the polypeptide chain is termed the primary structure. The primary structure is unique to a given protein. The primary structure can fold regularly to form either an α-helix or β-pleated sheet. The secondary structure is held together by hydrogen bonds between adjacent peptide bonds. The primary structure can further fold to form an overall three dimensional shape that more specifically determines the biological functions of the individual protein. This 3D structure is held together by bonds formed between the R-groups of amino acids. The bonds include hydrogen, ionic or disulphide bridges. These bonds give a greater strength to the molecule allowing it to withstand some variations in temperature or PH. A key role for proteins is to act as enzymes; biological catalysts that lower activation energy of specific reactions. They have an active site that has a specific three-dimensional shape that is complementary shape to a given substrate. This provides specificity to reactions. On binding, the enzyme and substrate form an enzyme-substrate complex which places strain on the bonds allowing them to break more easily. For example, the enzyme sucrase has an active site that is complementary to the disaccharide sucrose. Lactose, another disaccharide that has a similar but subtly different shape to sucrose, will not fit into this site, and is therefore not hydrolysed by the enzyme. DNA polymerase condenses adjacent DNA-nucleotides together during the formation of the sugar-phosphate backbone of DNA during semi-conservative replication. Despite

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