Genome research has made remarkable achievements since it was carried out. In the past few years, complete sequence analysis of genomic DNA of more than a dozen organisms with relatively simple structure, including e. coli, saccharomyces cerebrosaccharides and arabidopsis thaliana, has been successively completed. The genomic DNA sequencing of c. elegans has been completed. The much larger human genome project is expected to complete the sequencing of the entire genome's DNA by the beginning of this century. The flood of new genetic data has forced us to consider what the proteins encoded by these genes do. Not only that, the protein as the main carrier of biological functions, has its own unique activity rule, in the study of proteomics, cell protein synthesis is needed after subsequent conversion, these proteins tend to experience even after the translation of processing and modification, transshipment positioning, structure change, between protein and protein, and the interaction between proteins and other biological macromolecules.

In other words, instead of a single protein, a gene might have several or even dozens. So how does a cell that contains thousands or even tens of thousands of proteins work? Or how do these molecular weight of protein work, interact with and coordinate with each other in the cell? These questions are far more than the genome institute can answer. Because genomics has such limitations, it has prompted people to explore the composition and activity rules of cell proteins on an overall level.

With the completion of the human genome project and the arrival of the functional genome era, protein structure and function research has become increasingly important, and proteomics and protein identification service have gradually become the forefront of life science. Protein is the executor of physiological function and the direct embodiment of life phenomenon. The study of protein structure and function will directly clarify the change mechanism of life under physiological or pathological conditions. The existing forms and activities of proteins themselves, such as post-translational modification, protein-protein interaction and protein conformation, are still dependent on the study of proteins directly. Although the special properties of protein, such as variability and diversity, make the protein research technology much more complicated and difficult than the nucleic acid technology, it is these characteristics that participate in and affect the whole life process.

Although proteomics research is still in the initial stage, it has made some important progress. At present, the main content of proteomics is to carry out proteome analysis while establishing and developing the technical methods of proteome research. There are two main aspects of proteome analysis. On the one hand, two-dimensional gel electrophoresis is used to obtain the atlas of all proteins in the body, tissue or cell under normal physiological conditions, and the relevant data will be used as the two-dimensional reference atlas and database of the body, tissue or cell to be tested. A series of such two-dimensional reference maps and databases have been established and can be retrieved online. The significance of two-dimensional reference atlas is to provide a basis for further analysis. The other aspect of proteomic analysis is comparative analysis of what happens to the proteome under changed physiological conditions. For example, changes in Protein Quantification, changes in posttranslational modifications, or changes in Protein localization at the subcellular level under possible conditions.  

Proteomics emphasizes a holistic approach to proteins. From the perspective of the whole, proteome research can be roughly divided into two types: one is to focus on the whole protein of cells or tissues, that is, the whole proteome. The other approach is to look at all the proteins involved in a particular biological problem or mechanism, where the whole is local. For cell proteome analysis of the complete work has been more comprehensive, not only in inferior patterns such as e. coli, yeast protein group in the database, higher organisms such as rice and mice the proteome research have been carried out, some human proteome database of normal and diseased cells are also building. At the same time, more proteome studies focus on the changes or differences of proteome, that is, through comparative analysis of proteome, the first discovery and identification of protein components with differences in proteome under different physiological conditions or different external environmental conditions.

In general, protein spectrometry is a method used to identify a protein, while protein sequencing is actually the number of polypeptide chains in the detection of a protein, and it does not necessarily need to use mass spectrometry sequencing. To put it simply, there are many ways to sequence proteins, usually after the construction is completed, through sequencing to compare whether the previously predicted sequence is correct or not. Mass spectrometry is used to determine whether the protein was originally designed after protein expression is purified.

Although proteomics is still in a early stage of development, but believe that with its constant development, proteomics research in life activities such as growth, development and metabolic regulation will be a breakthrough, the law of to explore the mechanism of the major diseases, disease diagnosis, disease prevention and control, new drug development, the regulation mechanism of plant growth and development to provide important theoretical basis.

The research content of this academic direction can be divided into two aspects. The first aspect is the application of proteomics in medical research. Research in this field will help people find some identifiable proteins for medical use, which can be used as diagnostic markers or as diagnostic target molecules to provide to institutions engaged in medical and diagnostic research.