Exploring the Functions of Proteins

The common types of proteins are hormones and enzymes. The enzymes have the key function to act as catalyst in biochemical reaction and the hormones are referred to as chemical-signalling molecules that are secreted from the endocrine glands. The digestive enzymes such as amylase, trypsin, pepsin and others have the function to assist in digestion through catalysation of nutrients received from food into monomeric units (Li et al. 2018). The transport proteins such as albumin and haemoglobin have the function to carry lymph and blood through the entire body. The defence proteins such as immunoglobins have the function to protect the body from diseases by avoiding energy and attach of foreign pathogens (Krieger et al. 2015). If you are delving into the complexities of biochemistry and need guidance, consider seeking chemistry dissertation help to navigate through your academic journey seamlessly.

Polar and Non-polar Amino Acid:

Amino Acids are of two types which are polar and non-polar. The polar amino acid has side-chains which residues with an aqueous environment leading them to be present at the surface of the protein. (Eg: glutamic acid, aspartic acid and others). The non-polar amino acids are those in which the residue group is made up of mainly hydrocarbons. (Eg: Alanine, cystine, proline and others) (Mascarin et al. 2016)

Primary Protein Structure

The primary structure of protein is referred to the amino acid sequence in which they are linked in the polypeptide chain. The sequence includes α-carbon bonded with hydrogen atom at the first followed by carboxyl group, amino group and at the end an R or variable group. This structure of the protein is bound together with the assistance of peptide bonds which are formed during protein biosynthesis. One end of the primary protein structure is referred to as carboxyl terminus and another end as amino terminus. The R group in the structure is varied among amino acids and the amino acid sequence of the primary protein is determined by the genetic code present in the cell (Boll et al. 2017).

General structure of Amino Acid

The general structure of amino acid indicates that there is central carbon atom that is surrounded by a hydrogen atom along with carboxyl group, R-group and amino group. The R-side chain is a unique feature in all amino acids as they are different from one another. The side chains of the amino acids sometimes contain nitrogen or sulphur apart from carbon, hydrogen and oxygen in the R-groups

(Mascarin et al.

The peptide bond is referred to the chemical bond which is formed in the middle of two molecules when the α-amino group of one molecule and the α-carboxyl group of another molecule reacts between one another to release water. The process is a dehydration synthesis reaction and mainly happens in between amino acids (Hernández et al. 2017).

Secondary Protein Structure

The secondary structure of protein is referred to the folding of the polypeptide chain which leads the protein to provide a three-dimensional shape. The two secondary protein structures are α helix and β helix. In alpha (α) helixes, spiral spring is formed which is secured with the help of hydrogen bond present in the polypeptide chain. In beta (β) helixes the structure is found to be pleated or folded which is held with the help of hydrogen bond present in between polypeptide units of the chain lying adjacent

Tertiary Protein Structure

The tertiary structure of the protein is referred to the comprehensive three-dimensional shape of the polypeptide chain. In tertiary structure, there are different bonds which hold the protein in the shape one of which is hydrophobic interaction that offers assistance to the shaping and folding of the protein. In this bond, the hydrophilic R group tries to contact with the aqueous environment and the hydrophobic R groups in the amino acid avoid contact with water as well as try to position them in the central part of t

Quaternery Protein Structure

The quaternary structure of the protein is referred to the folding in which the protein macromolecule is developed through the interactions of various polypeptide chain. In the structure, the polypeptide chain is regarded as subunit (Leonard and Ahnert, 2019).

Globular Protein

The globular proteins are water-soluble and they execute the action by forming colloids in the water. One of the examples of globular protein is haemoglobin which has the key function to carry oxygen through the blood to different parts of the body (Damry et al. 2019).

The Fibrillar proteins are referred to the insoluble proteins which are mainly the principle protein present in the body. One of the examples of fibrillar protein is collagen which is found abundant in the body and has the main function is to provide support to the tissues in the body. The collagen is the key component of connective tissues that is present in the body in tendons, skins, ligaments and others (Knowles and Mezzenga, 2016).

polypeptide chains which function to hold the protein ion shape made through the assistance of hydrophobic interactions (Watkins et al. 2015). The ionic bonding mainly develops between the negative and positive R groups when coming in close contact. The covalent bonding occurring between R groups of amino acids and cystine helps in protein folding (Bai et al. 2015).

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