# Brief Outline on Protein Biophysical Characterization in Proteomics

Kim Robinson

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## To cite this version:

Kim Robinson. Brief Outline on Protein Biophysical Characterization in Proteomics. Cellular & Molecular Medicine: Open access, 2021, Brief Outline on Protein Biophysical Characterization in Proteomics, 7 (6). [https://doi.org/10.5540/pcbm.2021.7.6.2229](https://doi.org/10.5540/pcbm.2021.7.6.2229)

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# Brief Outline on Protein Biophysical Characterization in Proteomics

Kim Robinson*

**Received:** October 08, 2021, **Accepted:** October 12, 2021, **Published:** October 19, 2021

Editorial office, Cellular and Molecular Medicine: Open access, UK

## Editorial Note

Proteomics is the study of vast numbers of proteins' expression, structure, relationships, and, to some extent, function at a high throughput level. A quantitative description of the stoichiometry, kinetics, and energetics of each protein complex in a biological pathway is also required for a true understanding of the functioning of a living cell. Traditional molecular biophysical studies help to understand these precise features of proteins on a smaller scale than proteomics, which focuses on individual proteins. Traditional molecular biophysical studies help to understand these precise features of proteins on a smaller scale than proteomics, which focuses on individual proteins. The role of biophysical approaches in the study of proteins in the proteomic era is discussed in this perspective piece. Several significant physical biochemical approaches are briefly addressed and criticised in terms of data collecting and information content. The emphasis is on conformational changes and macromolecular assembly, as well as the value of dynamic and static structural data and the need to combine experimental methodologies in order to achieve a complete functional description. Proteomics is the study of all proteins (and alternatively spliced varieties) expressed by a genome, as well as their isolation, identification, structural determination (with post-translational modifications), interaction with partners (other proteins, lipids, nucleic acids), expression, developmental time courses, effects on biological responses, and functional properties. The use of high-throughput technologies that approach the real concurrent accumulation of these data is implicit in this concept. In practise, a proteomic methodology may concentrate on a more constricted proteome from cell fractionation, such as that supplement related to a cellular organelle (e.g. mitochondria), or, unlike a genomic approach, may focus on a more restricted proteome from cell phase separation, including that correlate pertaining to a cells organelle (e.g. mitochondria, nucleosome). In the race to gather high throughput protein structures or to uncover interatomic, the determination of the ground rules that regulate function is sometimes overlooked; yet, many investigators stress the significance of a quantitative assessment of function. Much of the high throughput strategy implies that discovery-based

*Corresponding author: Kim Robinson

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cellmolmed@journalres.com

Cellular and Molecular Medicine: Open access, UK

**Citation:** Robinson K (2021) Brief Outline on Protein Biophysical Characterization in Proteomics. Cell Mol Med. Vol. 7 No. 5: 24.

research will outperform hypothesis-driven experiments as a means of scientific advancement, which is a source of debate. Separation (two-dimensional gels, liquid chromatography, mass spectrometry), structure (x-ray and NMR), and interactions (mass spectrometry, yeast two-hybrid, immunoprecipitations, combinatorial methods) have dominated proteomics research, with a shift toward studying hundreds or thousands of proteins at a time. A quantitative, dynamic explanation of the stoichiometry, the kinetics of formation, the energetics of formation, and the functional ramifications of each protein complex in a cellular pathway is also required for a really erudite, comprehensive grasp of the functioning of a live cell. Since the period of viscosity measurements and sedimentation analysis in the analytical centrifuge, traditional biophysical analysis has been used to determine the size, shape, and solution properties of proteins. Proteins were first defined as specified globular or fibrous proteins with exact composition, suitable to a more sophisticated structural investigation at the atomic level, thanks to biophysical studies in the first part of the twentieth century. Biophysical techniques can give insights into how proteins function in solution and interact dynamically with one another, in addition to exact molecular protein structures obtained by crystallography and high resolution NMR. Hydrodynamic methods (analytical ultra-centrifugation, Viscometry, etc.), Thermodynamic methods (light scattering, micro calorimetry, surface plasma resonance), and spectroscopy fluorescence, Circular Dichroism (CD), Electron Para Magnetism (EPR) are among the techniques that can be used.