Journal of Proteomics & Bioinformatics
Open Access

Protein Characterization and Structure Identification through Proteomics

Isabel Sandra^{* *}Correspondence: Isabel Sandra, Research Institute for Chromatography (RIC), Howest University , Kortrijk, Belgium, Email:

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Description

Protein characterization plays a role in two key aspects of structural proteomics. The first is the evaluation of the protein preparation quality after production. One of the main obstacles in the pipeline for determining the structure of crystals is their ability to diffract light well. There are two methods commonly used to identify proteins, Edman Degradation (ED) and mass spectrometry. The determination of protein properties, such as domains, oligomeric state, post-translational modifications, and interactions between proteins and their ligands, is the second aspect. Proteins control gene activity and regulate gene expression. In the post-genomic era proteomics will make a significant contribution to our comprehension of how genes work. Proteins are essential components of living organisms, performing numerous functions such as the formation of structural fibers in muscle tissue, enzymatic digestion of food, and DNA synthesis and replication. Protein characterization is important because proteins provide many of the structural elements of cells and help to hold them together and organized. Proteins protect animals from disease in the form of antibodies. Many hormones are proteins. Proteomics can be broken down into three main categories:

• Protein micro-characterization, which identifies proteins and their post-translational modifications on a large scale

• "Differential display" proteomics, which compares protein levels and may be used to treat a variety of diseases

• Study on protein-protein interactions, which use methods like mass spectrometry or the yeast two-hybrid system

The determination of the components of a protein complex or of a cellular structure is crucial in functional analysis because it is frequently challenging to anticipate the function of a protein based on homology to other proteins or even their threedimensional shape. This field of proteome research holds the most potential, arguably.

Different sets of proteins may be produced by a cell at different times or under different conditions, such as during development, cellular differentiation, the cell cycle, or carcinogenesis. Most proteins can undergo a wide range of post-translational modifications, further increasing proteome complexity. When looking for a biomarker for a specific cancer subtype, the proteomics scientist may choose to study multiple blood serum samples from multiple cancer patients to reduce confounding factors and account for experimental noise. As a result, complicated experimental characteristic of proteins are required to identify the structure of the proteome's dynamic complexity.

There are numerous methods for studying proteins in proteomics. Proteins can generally be detected using antibodies (immunoassays), electrophoretic separation, or mass spectrometry. Because there are too many analytes in the sample to perform accurate detection and quantification, a very specific antibody must be used in Quantitative Dot Blot (QDB) analysis, or biochemical separation must be used before the detection step.

In the current post-genomic, systems biology methods to understanding molecular mechanisms underpinning healthy and disease phenotypes, as well as identifying crucial diagnostic and prognostic biomarkers, proteomics is a fundamental tool. As a result, proteomics aims to evaluate protein quantity, location, posttranslational modifications, isoforms, and molecular interactions in addition to identifying proteins that may be present in a sample. With an emphasis on high throughput and minimal user bias, the field of proteomics has developed at the intersection of physics and biology, computer science, and bioinformatics. As a result, a variety of technologies are employed, but coupled techniques such as liquid chromatography and Mass Spectrometry (MS) or one- or twodimensional gel electrophoresis are virtually always used.

Although mass spectrometry and microarray provide peptide fragmentation information, they do not identify specific proteins present in the original sample. Previous researchers were forced to search the peptide fragments themselves due to a lack of techniques for specific protein identification. However, programmes for protein identification are currently available and more and more studies are going on over these techniques as well. The programme implements algorithms that perform alignments with proteins from known databases such as Uni Protein and PROSITE to predict what proteins are in the sample with a high degree of certainty. Protein characterization is the method used to identify the proteins present in cellular and biological samples after mass spectrometry analysis. Protein characterization is crucial for establishing the efficacy and safety of biological products, thus it's important to keep improving the accuracy, sensitivity, and durability of protein assays as well as creating new assays that focus on particular problems.