Chromatographic separation strategies for precision mass spectrometry to study protein-protein interactions and protein phosphorylation.
Authors of this article are:
Minic Z, Dahms TES, Babu M.
A summary of the article is shown below:
Investigating protein-protein interactions and protein phosphorylation can be of great significance when studying biological processes and human diseases at the molecular level. However, sample complexity, presence of low abundance proteins, and dynamic nature of the proteins often impede in achieving sufficient analytical depth in proteomics research. In this regard, chromatographic separation methodologies have played a vital role in the identification and quantification of proteins in complex sample mixtures. The combination of peptide and protein fractionation techniques with advanced high-performance mass spectrometry has allowed the researchers to successfully study the protein-protein interactions and protein phosphorylation. Several new fractionation strategies for large scale analysis of proteins and peptides have been developed to study protein-protein interactions and protein phosphorylation. These emerging chromatography methodologies have enabled the identification of several hundred protein complexes and even thousands of phosphorylation sites in a single study. In this review, we focus on current workflow strategies and chromatographic tools, highlighting their advantages and disadvantages, and examining their associated challenges and future potential.
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This article is a good source of information and a good way to become familiar with topics such as:
Liquid chromatography;Precision mass spectrometry;Protein phosphorylation;Protein-protein interactions;Proteomic workflow;Systems analysis
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