Function of Protein

Introduction

Proteins vary in shape and molecular weight, some are globular in shape, while others are fibrous in nature.Hemoglobin, for example, is a globular protein, whereas collagen, which is found in our skin, is a fibrous protein.Protein shape is critical to its function, and it is maintained by a variety of chemical bonds.Temperature, pH, and chemical exposure can cause permanent changes in the shape of the protein, resulting in loss of function, a process known as denaturation. Protein serves numerous functions in your body,It aids in the repair and growth of your body’s tissues, allows metabolic reactions to occur, and coordinates bodily functions.Proteins not only serve as a structural basis for your body, but they also serve as a source of energy and also maintain proper pH and fluid balance.

Proteins are involved in a wide range of critical biological processes and functions. They are extremely versatile and serve a variety of functions in the body, as listed below:

•Provide mechanical support

•Provide immune protection

•Generate movement

•Transmit nerve impulses

•Act as catalysts

•Transport other molecules

•Store other molecules

•Control cell growth and differentiation

Types of Protein

Two special and common types of proteins are enzymes and hormones.

1. Enzymes are complex or conjugated proteins that are produced by living cells and act as catalysts in biological reactions (such as digestion).Each enzyme acts on a specific substrate (a reactant that binds to the enzyme).The enzyme could aid in reactions involving breakdown, rearrangement, or synthesis. Catabolic enzymes break down their substrates, anabolic enzymes produce more complex molecules from their substrates, and catalytic enzymes influence the rate of reaction.All enzymes, it should be remembered, improve the pace of reaction and are thus classified as organic catalysts. Salivary amylase, for example, hydrolyzes amylose, a component of starch, as its substrate.

2. Hormones are chemical-signaling molecules that are produced by endocrine cells and act to control or regulate particular physiological processes such as growth, development, metabolism, and reproduction. Insulin, for example, is a protein hormone that aids in the regulation of blood glucose levels.

Primary protein structure

A long chain of amino acids makes up proteins. Even with a small number of amino acid monomers – there are only about 20 in the human body – they can be organized in a variety of ways to change the protein’s three-dimensional structure and function. The fundamental structure of a protein is its simple sequencing. Hemoglobin is an example of a protein with a primary structure. This protein, which is present on red blood cells, helps in the delivery of oxygen to all of your body’s tissues.

Secondary protein structure

Local interactions between portions of a protein chain influence secondary protein structure, which can impact the folding and three-dimensional shape of the protein. The secondary structure can be altered by two key factors.

•α-helix: The backbone’s N-H groups make a hydrogen connection with the C=O group of the amino acid 4 residues earlier in the helix.

•β-pleated sheet: Hydrogen bonds arise between N-H groups in one strand’s backbone and C=O groups in the backbone of a fully expanded strand adjacent to it.

Each and every protein may also be linked to lots of functional groups such as alcohols, carboxamides, carboxylic acids, thioesters, thiols, and other basic groups.These functional groups also influence protein folding and, as a result, bodily function. Silk proteins, is an example of secondary structure having a beta sheet structure. A nucleic acid, such as tRNA’s clover leaf structure, is another example of a secondary structure.

Tertiary protein structure

After secondary interactions, proteins’ tertiary structure is said to be their total 3D shape. These involve the effects of the protein’s polar, acidic,non polar and basic R groups. Amide hydrogen atoms, for example, can form H-bonds with neighboring carbonyl oxygens.

Quaternary protein Structure

Quaternary protein structure refers to the orientation and organization of subunits in multi-subunit proteins. Only proteins with numerous polypeptide chains are affected.Proteins fold up into certain shapes based on the amino acid sequence in the polymer, and the obtained three dimensional structure is closely tied to the function of protein.

Proteins have a wide range of properties. Some are fairly hard, while others are a little more flexible. These traits are also consistent with the protein’s function. More rigid proteins, for example, may have a role in the cytoskeleton or connective tissue structure. Those with some flexibility, on the other hand, can operate as hinges, springs, or levers to help other proteins function. Hemoglobin, DNA polymerase, ribosomes, antibodies, and ion channels are examples of proteins containing quaternary structure.

Conclusion

Proteins are a type of macromolecule that helps the cell conduct a wide range of tasks. They aid metabolism by serving as enzymes, transporters, or hormones as well as providing structural support.Amino acids are the building elements of proteins (monomers). A core carbon is linked to an amino group, a carboxyl group, a hydrogen atom, and a R group or side chain in each amino acid. There are 20 amino acids that are regularly found in nature, each of which differs in the R group. A peptide bond connects each amino acid to its neighbors. Polypeptides are made up of a lengthy sequence of amino acids.Primary, secondary, tertiary, and (optional) quaternary are the four levels at which proteins are organized. The primary structure is the sequence of amino acids that is unique. The secondary structure is formed by the polypeptide folding locally to generate structures such as a helix and a B-pleated sheet.The tertiary structure is the overall three-dimensional structure. The quaternary structure of a protein is created when two or more polypeptides unite to produce the entire protein structure. Protein form and function are inextricably related, any change in shape caused by temperature or pH changes can result in protein denaturation and loss of function.