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Commentary Article - (2023) Volume 9, Issue 1

Study of Protein Structure and its Function of Biomolecules and Macromolecules
Toya Gurung*
Department of Biochemistry, Tribhuvan University, Nepal
*Correspondence: Toya Gurung, Department of Biochemistry, Tribhuvan University, Nepal, Email:

Received: 30-Jan-2023, Manuscript No. IPBMBJ-23-16009; Editor assigned: 01-Feb-2023, Pre QC No. IPBMBJ-23-16009 (PQ); Reviewed: 15-Feb-2023, QC No. IPBMBJ-23-16009; Revised: 20-Feb-2023, Manuscript No. IPBMBJ-23-16009 (R); Published: 27-Feb-2023, DOI: 10.36648/2471-8084-9.01.07


Proteins are substantial biomolecules and macromolecules made up of one or more long chains of amino acid residues. A few of the numerous functions that proteins do within animals include facilitating metabolic processes, reproducing DNA, reacting to stimuli, providing cells and organisms with shape, and transporting materials. Proteins differ from one another primarily in how their amino acid grouping is organized. This arrangement is determined by the nucleotide succession of the amino acids, and it typically results in the protein compressing into a specific 3D design that determines its mobility. A linear chain of amino corrosive deposits is known as a polypeptide. Peptides are the usual name for small polypeptides with fewer than 20-30 residues. Rarely are they regarded as proteins. The individual amino acid residues are linked together by peptide bonds and nearby amino acid residues. The sequence of amino acid residues of a protein is determined by the sequence of a gene, which is encoded in the genetic code. The genetic code typically lists 20 standard amino acids; however, some organisms’ genetic codes may incorporate pyrrolysine and selenocysteine, respectively, in some archaea. By chemically modifying the residues in a protein shortly after or even during synthesis, post-translational modification modifies the physical and chemical characteristics, folding, stability, activity, and, ultimately, function of proteins. Certain proteins contain non-peptide groups, also referred to as cofactors or prosthetic groups. Proteins can also cooperate with one another to complete a specific purpose, and they regularly band together to create stable protein complexes. Proteins only exist for a brief time after they are created, and the machinery of the cell uses the process of protein turnover to break them down and recycle them. The variable lifespan of a protein is determined by its half-life. They can exist in mammalian cells for minutes or years, with a typical lifespan of one to two days. Because they are unstable or because they are specifically targeted for lysis, aberrant or misfolded proteins breakdown more quickly.

Like other biological macromolecules like polysaccharides and nucleic acids, proteins are crucial parts of organisms and are involved in almost every cell-to-cell process. Many proteins are enzymes that catalyse biological reactions and are essential for metabolism. Actin and myosin, which are found in muscles, are examples of proteins that perform structural or mechanical tasks. The cytoskeleton, a system of scaffolding that keeps cells in their proper shape, is made up of proteins. Proteins play important roles in the cell cycle, cell bonding, safe reactions, and cell flagging. Animals use proteins to obtain the required amino acids that they cannot produce on their own. Digestion breaks down proteins for use in metabolism.


All proteinogenic amino acids have common basic components, containing α-element at which point an amino assemblage, a carboxyl assemblage, and a changeable side chain are supported. Only proline clashes from this fundamental building cause it has an idiosyncratic ring attributed to the N-end amine group. This ring forces the CO-NH amide subdivision into an established shape that is reason proline is singular. The list of standard amino acids investigates detail about the side chains, that have an expansive range of synthetic forms and possessions; a protein’s three-spatial structure and synthetic sensitivity are eventually contingent upon the accruing effect of all of allure amino acid side chains.


The author is grateful to the journal editor and the anonymous reviewers for their helpful comments and suggestions.

Conflict of Interest

The author declared no potential conflicts of interest for the research, authorship, and/or publication of this article.

Citation: Gurung T (2023) Study of Protein Structure and its Function of Biomolecules and Macromolecules. Biochem Mol Biol J.9:07.

Copyright: © 2023 Gurung T. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.