Proteins are large molecules, also known as polypeptide chains which are folded to form a three-dimensional structure. They consist of at least one amino acid residues (Wikipedia, n.d) and they have one of the most complicated structures (Alberts, et al., 2002) amongst the molecules. Proteins have four different levels of …show more content…
Denaturation is the process whereby the shape of the protein is disrupted, leading to the change in chemical and physical properties of the properties. In some cases, there may also be some loss of biological activity. However, the primary structure will not be disrupted when a protein denature as a large amount of energy is needed to break down the relatively strong peptide bonds in the primary structure. Some of the factors resulting in the denaturation of proteins are heat and change in pH or potential of hydrogen. An increase in temperature will disrupt the weak forces of attraction between the R groups such as hydrogen bonds, Van der Waales forces and induced dipole-induced dipole attractions. The application of heat on the protein will increase the kinetic energy of the molecules leading to the breakage of the bonds. Thus the stability of the secondary, tertiary and quaternary structures will be weakened as well. Proteins will coagulate with denaturation and they will no longer be able to catalyse reactions as well. Changes in pH will result in the reaction between H+ and OH- ions with the basic and acidic R groups respectively. This will then disrupt the ionic bonds in both the tertiary and quaternary structures. If extremely high temperature is applied to the protein or if it is placed in a very acidic or basic environment, denaturation will be …show more content…
Neurodegeneration refers to the condition affecting the neurons (Przedborski et al., 2003) and the gradual loss of neural cells which will result in a malfunctioned nervous system (Brown, 2005). It has been widely agreed and found that proteins in the bodies of those suffering from the above diseases are abnormally folded (Ross and Poirier, 2004). Large amounts of aggregated proteins present in cells will lead to abnormal folding of proteins and the disruption of the polypeptide’s structure which will in turn result in the loss of the function of the nervous system (Tutar et al., 2013). Moreover, proteins are very vulnerable to other forces such as mutations and protein-protein interactions. Also, new proteins have a tendency to fold incorrectly and due to the above reasons, proteins will most likely aggregate (Tutar et al., 2013). With that, I conclude that proteins are essential in carrying out almost all of the functions in our body and the aggregation or misfolding of these proteins may cause neurodegenerative diseases. These diseases will lead to the death of our cells and have negative consequences on our motor skills as our muscles will be