How is Protein Structure related to its function?

Proteins are fundamental compounds which are highly important in our lives, from catalysing reactions to even aiding transport - all in which keeps us alive. Proteins are synthesised in the ribosome's of cells by use of nuclear DNA which codes for certain amino acids. Proteins have four different type of structures; primary, secondary, tertiary and quaternary. The amino acids form a protein by a condensation reaction between adjacent amino acids forming peptide linkages which is also known as the primary structure of a protein (sequence of amino acids). The secondary structure of a protein is dependent on the amino acids of the polypeptide as this will determine whether the polypeptide folds to from -pleated sheets or twist to form an -helix. The tertiary structure is again dependent on the secondary structure of the protein as the protein complex twists/folds even more to form either a globular protein (-helix) or fibrous protein(-pleated sheets). Fibrous proteins, such as keratin in nails, are strong chains of polypeptides whereas globular proteins, such as enzymes, are more spherical with a very large surface area. The large surface area in globular proteins is vital to its function as explained in the next paragraph. Enzymes are biological catalysts which are surface acting . They reduce the activation energy of a reaction by distorting the Intramolecular bonds in the substrate thus making it easier to hydrolyse. Furthermore, enzymes are not used up in reactions so can therefore be recycled for continuous use as well as it forms a tighter fit. This is called the induced fit model. The model proposes that the initial interaction between enzyme and substrate is relatively weak however these interactions induce a conformational change causing the substrate to adjust its shape slightly and the enzyme moulds onto the altered substrate to form a tighter fit and a faster catalysed reaction. As aforementioned, enzymes are examples of globular proteins and this is key to its function as it increases their surface area therefore the rate of reaction increases (rate surface area). Enzymes structure are affected by many external environments such as too high of a temperature, results in hydrogen bonds breaking thus the tertiary structure of the enzyme alters therefore the enzyme denatures. Another factor is pH, which changes the charge on the carboxyl and amine functional group thus altering its stability and its active site as the formation of hydrogen bonds change. Enzymes are used in many biological processes in the human body ranging from respiration to digestion. Also, the sequence of amino acids, which conforms to a polypeptide chain, causes a specific active site to be generated in which only a certain shaped-substrate will be complementary and then form a enzyme-substrate complex. However due to the structure of an enzyme, there can be more than one binding place( excluding the active site), also known as an allosteric site, which can either activate or even inhibit the enzymes role. These catalysts also come in many forms- a key example being transferase. These are found in abundance at presynaptic neurones and are used, in this example, to reform neurotransmitters i.e. choline acetyltransferase recombines acetyl and choline back to acetylcholine. Another very important protein that is fundamental in out fight against diseases, are antibodies. These proteins, also known as immunoglobulin's, are in the form of a large Y-shape which is produced in vast amounts by B-lymphocyte cells, most specifically plasma cells. They are used by the

immune system to identify and neutralise foreign objects such as pathogens. They do this by recognising a unique part of the foreign body called the antigen and like the enzyme, it has a specific antigen-binding site which is only complementary to a certain antigen. This means that specific diseases can be targeted for a much faster immune response. In terms of the structure of the antibody, it composes of 2 heavy chains and 2 light chains bonded together by disulfide bonds. Antibodies can come in different varieties known as isotypes- A , G , M , E and D. These isotypes may be structurally different i.e. some isotypes can be just a single antibody known as a monomer, others can be a dimer or even a pentamer (5 different antibodies). Due to antibodies being very specific, they have recently been introduced in to the medical field by a term called monoclonal antibodies. These antibodies are very unique as they are being used at the moment for identifying as wells as treating different sorts of cancer. The final proteins which I will discuss about are both found in the phospholipid-bilayer of cell membranes - carrier proteins and receptors. Carrier proteins are examples intrinsic proteins which crosses through the cell membrane. What makes them highly adaptive is that not only can they be specific with regards to active transport, but they can also be voltage gated which are found in neurones and because of the variety of functions it can carry out, it becomes a fundamental part to many living processes. Carrier proteins as are used everywhere in the body as a mean of transferring substances in and out of the cell efficiently especially if the molecules are polar like ions. Furthermore what makes them very beneficial is that they are not situated in one area of the cell membrane - they can move around the phospholipid bilayer which is also known as the fluid mosaic model. Receptors are examples of extrinsic proteins usually found on the surface of cell membranes. There are many uses of receptors in the body ranging from a source of identification ( to prove that cell is not foreign) to an initiator at neuromuscular junction or for a hormonal response. As mentioned in the previous paragraphs, antibodies are proteins and how they differentiate between a foreign body and a body cell of the organism is by the receptor protein and this will initiate a immune response if it is deemed foreign. Receptors are used a lot at neuromuscular junctions as they are mostly found on the postsynaptic neurone and they usually have two binding sites for the neurotransmitter to adhere to thus causing Na+ ions to move in causing depolarisation of the axon therefore the action potential continues. Different receptors carry out different responses for example, morphine which is an narcotic analgesic opiate drug and it effects certain opiate receptors found mostly in the CNS. Morphine acts as an endogenous opiod which are endorphins and enkephalins. These chemicals bind onto a opiate receptor that ultimately leads to "inhibiting inhibition" therefore increasing dopamine concentrations. The dopamine reduces the pain by converting the pain signal to a calm and elate impulse thus symptoms of pain are reduced. The reason why morphine works is because the endogenous opiods are analogous, i.e. have structures with similar function but different origin thus allowing morphine to work in a similar way. In conclusion, the function of proteins is directly proportional to its active role in any biological process and it enhances the efficiency of certain processes which provide us with the nutrients to survive in the future.