Monomers of the amino acids form numerous chains of short sized and these chains are linked together with the help of peptide or amide bonds. These short chains are known as Peptides. When a group of amino acid involves in reaction with another group of amino acid of carboxyl group, the result of that reaction is the formation of covalent chemical bonds. In the domain of peptides, dipeptides are the shortest form of peptides as dipeptides are only consist of a peptide bond, which joins the 2 amino acids followed by tetra-peptides, tri-peptides and others.
Polypeptides are mainly a continuous, unbranched and long chain of peptides. Thus, peptides can be described as something, which comes under the wide range of chemical classes that includes biological classes of polymers and oligomers along with the polysaccharides, oligosaccharides and nucleic acids. In other words, the polypeptides can be described as the chains that consist of essential protein portions and amino acids. In the case of cells to function properly, one of the most important ingredient is the proteins. A cell consists of protein in such amount that proteins take up more than half of the cell’s total mass. Substances are stored and transported in cell with the help of proteins along with helping the cell with structuring support. Metabolic functions are control by the help of proteins. The cell with the help of proteins van defend itself from the various outside viruses. The structure of the proteins is very complex and diverse in nature. The functions of the polypeptides come in to the picture as every protein type holds unique and specific shape. Numerous acids of amino group are bonded together to make up the proteins with the help of polypeptides. When two or more amount of polypeptides are bonded together, the result of the bonds are the creation of the proteins. There many types of proteins and as per their requirement and specific shape the used polypeptides are folded accordingly. Particular group of amino acids are similar to the polypeptides. The only exception in that is the bonding as the bonds of electron sharing or covalent are used. When a polypeptide is created the basic pillars or building blocks of the structure are the Amino acids. There are nearly a total of 20 amino acids and they are all different than others. All the amino acids have their own unique and specific structures. When the idea and understanding of the structure of the amino acids are known, then the protein that are being built, the clear idea of the bond that the amino acids are going to use while bonding with other amino acids can be grasped easily. The appearance of the carboxyl groups are everywhere in amino acids. With the help of the carboxyl group, a group of negative is created thus, allowing the negative group to be bonded by another atom of carbon, which in result forms a covalent bond. Then the amino acid is created when this particular group goes bonding with a group of amino. While forming the proteins, the complexity and the diversity of the polypeptides are increased. Every polypeptide has two ends in which one end have the carboxyl group and the other have the amino group. One end of the polypeptide is known as the c-terminal, the end that consists of carboxyl group and the other end is known as the n-terminal, the end that consists of amino group.
The formation of polypeptides are an easy process. The process is kind of a wet process because of the involvement of the water. The amino acid groups are mainly the amino acids and they look like NH2. The carboxyl group are also present and the symbol is COOH. At the beginning of the formation of the polypeptide as already mentioned before two amino acids are joined one after another. They both join with the help of carboxyl group and amino group. The joining is known as the peptide bond, which is also known as covalent bond, which takes place between amino acids. The creation of the bond also releases some water. The whole procedure is also referred as the condensation bond as a large molecule is being formed with the combination of the two or more smaller molecules. The carboxyl group ends (COOH) are being reached by the amino acids, an OH is released and in the same way, when an amino group ends (NH2) are being reached by the amino acids, an H is released. Thus, when the released OH and H reacted with each other H2O is formed which is the released water.
The structure of the polypeptide consists four-leveled structure. The level of structures are the primary, secondary, tertiary and quaternary. The initial or primary structure determines or defines the rest of the structures.
Primary structure: In this structure, the chain of polypeptide is consists of sequenced amino acids. Any disulfide bonds locations are referenced with the amino acids. All the covalent bonding that present in polypeptide chain can be described by the primary structure. The most common way that the primary structure can be denoted is by writing the abbreviations of the amino acids that are used in sequence. Three letter abbreviations are used such as gly-gly-ser-ala, which is the glycine-composed polypeptide’s structure.
Secondary structure: Polypeptide’s localized region arranges or conforms the secondary structure in ordered manner. These folding patterns are not stabilized and hydrogen bonding helps to stabilize them. Anti-parallel beta-pleated sheet and alpha helix are the two main structures that are present in the secondary structure. These two are most stable among other available periodic conformations.
Tertiary structure: When the atoms of the polypeptide chain are three dimensionally arranged they form the tertiary structure. Polypeptides that only includes one kind of conformational folding pattern, which is also single such as only alpha helix, then the tertiary and the secondary structures are the same thing. Disulfide bonds maintains the tertiary structure largely.
Quaternary structure: In case of proteins consisting more than one subunits, which is the polypeptide chain, the structures of the proteins are described by the quaternary structure. The subunits in the quaternary structure are stabilized because of the force of hydrophobic interaction.
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