What Are Four Functions Of Proteins – Have you ever wondered why athletes or gymnasts often follow a protein-rich diet? Because these people spend more energy than people who don’t play sports. And a protein-rich diet nourishes the body to build muscle, support rapid recovery, boost immunity, replenish glycogen, and burn fat; all of which are important during strenuous exercise.
But is it only necessary for exercisers? No, protein has a myriad of roles to play in all living things. It is one of the basic macronutrients synthesized by organisms that are essential for a healthy life.
What Are Four Functions Of Proteins
This article is about proteins, their types, and the differences between them. It also covers the functions of proteins in living organisms and the methods of studying these molecules in laboratory conditions.
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Proteins are one of the versatile macromolecules in living organisms, performing key functions in various biological processes.
They are found throughout the body of organisms – muscles, bones, skin, hair and almost every part of the body or tissue.
They consist of 20 amino acids arranged in various structural forms, creating about 10,000 (or even more) proteins.
Proteins are built linearly from 20 amino acids, a repetitive process in the cell. However, the linear/primary sequence of the protein is not responsible for its functional roles.
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The sequences spontaneously assemble into various arrangements, forming three-dimensional structures defined by the amino acids present in the sequence. And these folded structures facilitate the functions of these proteins.
The most dominant functional groups found in proteins are alcohols, thiols, thioethers, carboxylic acids, carboxamides and various basic groups.
These functional groups linked in various random patterns in the amino acid sequence create a broad spectrum of protein functions. Put simply, the properties of the functional groups of proteins determine their enzymatic and other metabolic functions in the body.
Proteins interact with other proteins or biomolecules to perform tasks that they themselves do not have. Examples of such tasks are DNA replication, intracellular signaling and other complex basic biological processes.
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Rigid proteins (having tightly packed structures that restrict any movement or movement) are involved in the structural formation of cells, such as the cytoskeleton that forms the internal scaffolding within cells.
Flexible proteins (having loosely coupled structures that can be easily rearranged or moved as needed) act as hinges, springs and levers, performing essential functions and forming complexes with other proteins and macromolecules.
The process of protein synthesis is called translation. In this process, the mRNA codes are translated into the corresponding amino acids involved in protein formation. Each amino acid has its own unique nucleotide gene sequence. The amino acid genetic code consists of three sets of nucleotides called codons.
The process begins with the transcription of DNA into pre-mRNA using RNA polymerase. The pre-mRNA is then modified to form the mature post-transcriptional mRNA.
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Ribosomes bind to the mRNA and use a codon (three nucleotides) that matches the anticodon found in the tRNA to synthesize the amino acid (transfer ribonucleic acid is an adapter molecule that helps decode the mRNA).
The four nucleotides, A (adenine), G (guanine), C (cytosine) and T (thymine) form different combinations of nucleotides to form different amino acids.
Chemical protein synthesis includes peptide synthesis, which uses strategies such as chemical ligation, Staudinger ligation, or other orthogonal chemical reactions to link synthetic peptides.
Here, peptides (a chain of 30-50 amino acids) are produced and joined together via amide or peptide bonds to form specific proteins.
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However, when it comes to producing a polypeptide chain of more than 300 amino acids, this is an inefficient technique. It should be noted that the chemical synthesis of a protein occurs from the C-terminus to the N-terminus, while in biological processes, the synthesis occurs in the opposite direction, i.e. from the N-terminus to the C-terminus.
Proteins are made by linking two or more amino acid residues together in different directions or configurations. The amino acids in proteins are linked by peptide bonds formed by a condensation reaction between two amino acids during which water molecules are released.
The definition of protein structure may sound similar to peptides, but there is a fine line between proteins and peptides as both differ in size, structure and function as explained below:
As a result of different chemical interactions in its structure, different levels of protein structure are possible. For example, the assembly of a linear sequence of amino acids into three-dimensional structures is driven by several non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic interactions.
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The basic structure is the arrangement of amino acids into a linear polypeptide chain. Here, the amino acids are only linked by peptide bonds and disulfide bonds. The sequence of amino acids in the polypeptide chain is responsible for the functions of proteins, which are determined by deciphering the genetic codes of proteins or their corresponding genes.
This occurs through the formation of hydrogen bonds between molecules and is the first step in the folding of polypeptides into a three-dimensional structural form, that is, before the tertiary and quaternary structures.
Here, the polypeptide chain folds into a three-dimensional space containing one or more domains. The alpha helix and beta sheets fold into a compact spherical structure driven by non-specific hydrophobic interactions.
In an aqueous environment, hydrophobic or non-polar groups move inside proteins while hydrophilic R groups are on the surface or outside of the structure.
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More than one polypeptide chain is involved in quaternary structure. Polypeptide chains may exist in multiple copies of the same or may differ in amino acid sequences. Weak interactions such as hydrogen bonds and London dispersion forces hold many polypeptides bound together to form a quaternary structure.
A well-known example of a quaternary structure is hemoglobin, which carries oxygen in the blood and consists of four peptide chains (two alpha chains and two beta chains) to form a tetramer.
In vivo techniques are used to study the functional role of proteins inside cells; in terms of understanding the mechanism of action of proteins in a specific environment, in vitro techniques are preferred; On the other hand, in silico is a computational method to study proteins, such as understanding the formation of protein complexes and structural determination.
Proteins are one of the basic biomolecules necessary to sustain life. They consist of amino acids arranged in four structural levels: primary, secondary, tertiary and quaternary.
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They differ from peptides on both a structural and functional level. Protein functions include molecule transport, structure formation, storage, and enzymatic roles, while peptides only affect the activity of other molecules.
The spectrum of protein functions in organisms has lured scientists’ brains towards the complexity of what they do, so scientists want to understand the molecule’s structure and mechanism of action. Some common tools used to study proteins are mass spectrometry, chromatography, circular dichroism, and spectrometry.
Working with proteins requires a high level of care and knowledge. And given its importance in organisms, scientists are trying to develop, synthesize and purify the molecule at an individual level for use in medicine. The field of proteomics also opens doors for young scientists to open up new possibilities and contribute to improving the quality of human life.
Anjali Singh is a freelance writer. Following her passion for science and research, she completed her Masters in Plant Biology and Biotechnology at the University of Hyderabad, India. He has a strong research background in plant science with expertise in molecular techniques, tissue culture and biochemical assays. In her free time outside of work, she enjoys reading fiction, sketching or writing poetry. In the future, she wants to pursue a doctorate in cancer biology while continuing her excellence as a science writer.
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