Perspective - (2022) Volume 8, Issue 12
Received: 30-Nov-2022, Manuscript No. IPBMBJ-23-15405; Editor assigned: 02-Dec-2022, Pre QC No. IPBMBJ-23-15405 (PQ); Reviewed: 16-Dec-2022, QC No. IPBMBJ-23-15405; Revised: 21-Dec-2022, Manuscript No. IPBMBJ-23-15405 (R); Published: 28-Dec-2022, DOI: 10.36648/2471-8084-8.12.109
The extensive study of proteins is known as proteomics. Proteins play a crucial role in many biological processes, including the synthesis and replication of DNA, the enzymatic digestion of food, and the formation of structural fibers in muscle tissue. Other types of proteins include hormones that transmit vital signals throughout the body and antibodies that shield an organism from infection. The entire collection of proteins produced or altered by an organism or system is known as the proteome. A growing number of proteins can be identified thanks to proteomics.
This shifts with time and particular necessities, or stresses, that a cell or organic entity goes through. The genetic data from a number of genome projects, including the Human Genome Project, have greatly benefited proteomics, an interdisciplinary field. An important part of functional genomics, it investigates proteomes from the overall level of protein structure, activity, and composition. Large-scale experimental analysis of proteins and proteomes is commonly referred to as proteomics, but protein purification and mass spectrometry are also frequently mentioned. After genomics and transcriptomics, proteomics is the subsequent stage in the investigation of natural frameworks. Because proteomes vary from cell to cell and occasionally, it is more complicated than genomics because an organism’s genome is relatively constant. Because distinct genes are expressed in various cell types, it is necessary to identify even the fundamental set of proteins produced by a cell. RNA analysis was used to examine this phenomenon in the past, and it was found that there was no correlation between protein content and RNA analysis. It is now known that mRNA is not always translated into protein, and the amount of protein produced for a given amount of mRNA is influenced by the physiological state of the cell and the gene it is transcribed from. Proteomics provides a direct measurement of the protein’s quantity and confirms its presence. After translation, many proteins also undergo a wide range of chemical modifications, in addition to the differences caused by mRNA translation. The most well-known and generally concentrated on post-translational changes incorporate phosphorylation and glycosylation. The protein’s function is dependent on many of these post-translational modifications. Phosphorylation, which occurs in the course of cell signaling and affects numerous enzymes and structural proteins, is one such modification. A protein becomes a target for binding or interacting with a distinct set of other proteins that recognize the phosphorylated domain when a phosphate is added to particular amino acids, most commonly serine and threonine mediated by serine-threonine kinases or, less frequently, tyrosine mediated by tyrosine kinases. Many “proteomic” endeavors are focused on identifying the set of phosphorylated proteins in a particular cell or tissue type under specific conditions because protein phosphorylation is one of the most studied protein modifications. The scientist is made aware of the possible signaling pathways that are operating in that situation by this. E3 ubiquitin ligases are enzymes that can bind ubiquitin, a small protein, to specific protein substrates. Understanding the regulation of protein pathways is made easier by identifying which proteins is poly-ubiquitinated.
As a result, this is yet another legitimate “proteomic” study. In a similar vein, once a researcher has identified the substrates that are ubiquitinated by each ligase, it is helpful to identify the ligases that are expressed in a particular cell type. During development, cellular differentiation, the cell cycle, or carcinogenesis, for example, a cell may produce distinct sets of proteins at distinct times or under distinct conditions. As previously stated, most proteins can undergo a wide range of post-translational modifications, further complicating the proteome.
The author is grateful to the journal editor and the anonymous reviewers for their helpful comments and suggestions.
The author declared no potential conflicts of interest for the research, authorship, and/or publication of this article.
Citation: Soueif A (2022) Study of Proteins and Limitations of Genomics and Proteomics. Biochem Mol Biol J. 8:109.
Copyright: © 2022 Soueif A. 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.
