Proteins play an integral role in the body’s biological processes since they are responsible for regulating biochemical reactions as well as transporting molecules from one point of the body to another (Chou, 2011). In the case of plans, proteins contribute to the photosynthetic conversion of light into growth, thus forming basis of the structures such as tendon, hair, and skin. Various definitions of proteins have been developed over the years.
For instance, they are considered to be substances comprising of amino acids, compounds, and elements such as nitrogen, carbon, oxygen, hydrogen and in some instances, Sulphur. In this case, examples of proteins include those found in beef. In biology, proteins are defined as molecules that are primarily composed of polymers of amino acids that have been joined together by peptide bonds (Monopoli et al., 2011). The major distinguishing factor between proteins and other substances such as fats and carbohydrates is former’s nitrogen composition.
2.0 PROTEIN COMPOSITION
Proteins are composed of amino acids linked together by peptide bonds, thus leading to the formation of a protein, otherwise known as, polypeptide. On their part, amino acids are composed of carboxylic acid (COOH), an amine group (NH2), and a carbon. Moreover, it contains the variable R group (Chou, 2011). Various types of protein structures exist, namely, primary, secondary, and tertiary.
The primary structure of proteins refers to the simplest type of the molecule. It is characterized by a simple linear chain of amino acids that are linked together to form a protein. On the other hand, the secondary structures exhibit more complexities and refer to a conformation of amino acids (Shannahan et al., 2013). The two major types of secondary structures of proteins include the α-helix and β-sheet. α-helices are considered to be right-handed and are identified by their resemblances to spiral staircases (Raterman et al., 2013). Moreover, they are stabilized by stabilized by hydrogen bonds. In the analysis of proteins, it is evident that some types of amino acids are more available in α-helices than others.
For instance, alanine which is a small amino acid is considered to more common in α-helices. On the other hand, the presence of Glycine is less common in this type of secondary structure (Monopoli et al., 2011). This can be attributed to the fact that the hydrogen bonds are internal with the R groups being external. Bulkier amino acids including proline are not present in the α-helix due to their ability to destabilize the structure (Wilhelm et al., 2014). There are two forms of β-sheets; parallel and anti-parallel with the former occurring when adjacent chains move in a similar direction. Anti-parallel is therefore evidenced by the opposite movements of such chains (Shannahan et al., 2013). Due to the distortion of hydrogen bonds,
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