Characteristics Of Protein Based Biopolymer And Its Application

834 words - 4 pages

Protein Characteristics and Its Suitability for Polymer Development
Proteins are prepared by basic unit called amino acids. The protein’s structure is broadly classified into four major categories which are called primary, secondary, tertiary and quaternary structure. The primary structure of a protein is a linear polymer with a string of amino acids coupled by peptide bonds. Secondary structures of proteins are usually very regular in their conformation and in point of fact, they are the spatial arrangements of primary structures. ‘Alpha Helices’ and ‘Beta Pleated Sheets’ are two types of secondary structures and they are majorly stabilized by hydrogen bonds. The tertiary structure of a protein is the three-dimensional structure and is stabilized by the series of hydrophobic amino acid residues and by disulphide bonds formed among two cysteine amino acid. While the tertiary structure with less disulphide bonds, which form weak, rigid structures that are bendable, but still tough and can oppose rupture such as hair and wool. Structures that contain more disulphide bonds lead to stronger, stiffer and harder structures. Quaternary Structure of protein is the arrangement of two or more chains, to form an entire unit. The interactions between the chains are not dissimilar from those in the tertiary structure, but are distinguished only by being an inter-chain rather than an intra-chain. The quaternary structure involves the clustering of numerous individual peptide chains into an ultimate shape. A range of bonding interactions, including salt bridges, hydrogen bonding, and disulphide bonds hold the a variety of chains into a particular geometry. There are two major categories of proteins with quaternary structure, i.e. fibrous and globular protein. Fibrous proteins such as the keratins in hair and wool are composed of coiled alpha helical protein chains with other various coils analogous. Alternatively, globular proteins may have an arrangement of the above types of structures and are predominantly clumped into a shape of a globe. Major examples include insulin, haemoglobin, and most enzymes.
Keratin is a protein that contains disulphide bonds and has an array of characteristics that ranges from a structurally robust, impact-resistant material (horn) to a simple waterproof layer (turtle shell). Keratin is together mechanically efficient in tension (wool) and compression (hooves) [32]. Keratins are found in hair, wool, claws, nails, skin, fur, hooves, beaks, feathers, horns, scales, actin and mysin in muscle tissues. The main differences in various keratins arise from their sulphur content. If there are many cysteine disulphide cross-links, then...

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