Before diving into what is Monomer of protein? We must first understand the history of monomers and the role they play in chemical composition. Well, all chemicals form by a high percentage of small monomeric structures. Monomers have also played a crucial role in the rise of the plastic age. Since we had an abundance of diverse chemical supplies at low costs, it fueled researchers to study monomers. These studies led to the development of hybrid materials through a technique in which different monomer structures join together via polarization and copolymerization. Also, During industrialization, the rise of petrochemical products was a direct result of the diversification of structures that further led to the development of organic chemistry. Now, let us dive into what is Monomer of protein bonds and protein monomer name?
The Monomers of Protein Bonds
So what is Monomer of protein bonds? All living organisms have cells, and these cells have several large molecules such as nucleic acids, polysaccharides, and proteins. These large molecules have even smaller structures or units by combining them in large quantities. We refer to these large numbers of small structures as monomers. The linking makes polymers or macromolecules of several monomers. This Monomer linking up to form the chain of molecules is only possible due to the presence of carbon and its valency properties. We can form a variety of chains of monomers, such as sugar monomers, nucleotides, and amino acids.
All living cells essentially require nucleic acids and protein in the life process. Did you know that proteins are composed of monomeric building blocks called amino acids? So we can say that proteins are made of monomers called amino acids. The process of polymerization forms them. These building blocks monomers of proteins are further crucial in the life processes. We are now able to produce protein-like polymers by controlling the conditions and performing polymerization of amino acids. By repeating this process, we produce sugars and nucleotides, which are comparatively easier to prepare than amino acids. Different biomolecules took form by utilizing this similar process. All these development aids in the field of bioengineering to develop a variety of biopolymers.
Proteins
Elements such as Oxygen, nitrogen, hydrogen, and carbon bond covalently to form proteins, and sulfur can also be present in some cases. Before getting into the structure of proteins, we must first understand the structure of their atoms. Globular structures are only possible due to the reverse direction of polypeptide chains which is a direct result of about a third of its residues in loops. We recognize these loops as a type of ordered secondary structures. These loops have classification according to the type of structure they connect and the number of residues.
Moreover, we know that proteins are made of monomers called amino acids. There are up to twenty amino acids or building blocks of protein that vary in atoms connected and the length of their carbon chain. So we can call protein monomer names as amino acids. Every amino acid consists of hydrogen, amine, R group, and the carboxyl group. The bonds formed covalently between various amino acids during the formation of proteins are known as peptide bonds. We use proteins to perform various crucial functions in our body, and most of these proteins are structural proteins.
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The structure of the protein contains mainly 4 monomer protein structures. We call them a quaternary structure, tertiary structure, secondary structure, and primary structure. In the primary structure, proteins coil into pleated sheets and helices. Also, the amino acids sequence determines the primary structure, whereas hydrogen bonds joining amino acids determine the secondary structure of proteins. In the secondary structure, a single protein has a helix or coiled shape structure with hydrogen bonds. It is only possible to break these hydrogen bonds by changing the surroundings such as induce high temperatures or increase acidic property. In the tertiary structure of the protein, the sulphur atoms in amino acids bond tightly via peptide bonds. Lastly, in quaternary structures, individual units are connected spatially.
Building Blocks Monomers of Proteins
Let us answer the question: what are the monomers of proteins called? The building blocks monomers of proteins are known as amino acids. In other words, the protein monomer name is amino acids. There are twenty types of amino acids and proteins are made of a combination of these amino acids. Furthermore, there are a few other types of building blocks of proteins depending upon the varying size of molecules. Generally, we categorize them as essential and non-essential building blocks of proteins depending upon their requirement. Also, we can make up to ninety thousand combinations or arrangements of proteins using these amino acids.
Additionally, nucleotides have the building blocks of nucleic acid chains.
FAQs on Monomeric Proteins
1. What are monomeric proteins as per the CBSE syllabus?
A monomeric protein is a protein that consists of only a single polypeptide chain. This single chain of amino acids folds into a specific three-dimensional shape, known as its tertiary structure, to become biologically active. Unlike multimeric proteins, they do not have a quaternary level of structure because they are not composed of multiple subunits.
2. What is a common example of a monomeric protein and its function?
A classic example of a monomeric protein studied in biology and chemistry is myoglobin. Its primary function is to bind and store oxygen within muscle cells, ensuring a reserve of oxygen is available for when the muscles are working hard. Its ability to hold oxygen is directly related to its specific folded tertiary structure.
3. What is the main difference between monomeric and multimeric proteins?
The fundamental difference lies in their composition and structural complexity. Here's a breakdown:
- Monomeric Proteins: Composed of a single polypeptide chain. Their highest level of structure is the tertiary structure. Example: Myoglobin.
- Multimeric Proteins: Composed of two or more polypeptide chains (called subunits). They exhibit a quaternary structure, which describes how these individual subunits are arranged. Example: Hemoglobin, which has four subunits.
4. What are the building blocks of proteins and how are they classified?
The building blocks, or monomers, of all proteins are amino acids. There are 20 common amino acids that make up proteins. Based on the body's ability to produce them, they are classified into two main types:
- Essential amino acids: These cannot be synthesized by the human body and must be obtained through diet. Examples include lysine, leucine, and valine.
- Non-essential amino acids: These can be synthesized by the human body from other compounds. Examples include alanine, glycine, and proline.
5. How does the structure of a monomeric protein determine its function?
The function of a monomeric protein is entirely dependent on its unique and highly specific three-dimensional tertiary structure. The folding of the single polypeptide chain creates specific regions, such as active sites in enzymes or binding pockets in transport proteins like myoglobin. Any disruption to this precise shape, through a process called denaturation, will destroy its biological function.
6. Can a monomeric protein have a quaternary structure? Explain why or why not.
No, a monomeric protein cannot have a quaternary structure. The definition of quaternary structure specifically refers to the spatial arrangement and interaction of multiple, separate polypeptide subunits. Since a monomeric protein, by definition, consists of only a single polypeptide chain, it lacks the necessary components for this level of organization. Its structural hierarchy stops at the tertiary level.
7. What happens when a monomeric protein like myoglobin is denatured?
When a monomeric protein such as myoglobin is denatured by factors like extreme heat or changes in pH, it loses its functional tertiary structure. The polypeptide chain unfolds from its precise, compact shape into a random coil. Although the primary sequence of amino acids remains intact, the destruction of the tertiary structure eliminates the oxygen-binding pocket, leading to a complete loss of its biological function.
