Separation methods for system‐wide profiling of protein terminome

Abstract

Protein N‐ and C‐termini have specific biochemical properties and functions. They play vital roles in various biological processes, such as protein stability and localization. In addition, post‐translational modifications and proteolytic processing generate different proteoforms at protein termini. In recent years, terminomics has attracted significant attention, and numerous strategies have been developed to achieve high‐throughput and global terminomics analysis. This review summarizes the recent protein N‐termini and C‐termini enrichment methods and their application in different samples. We also look ahead further application of terminomics in profiling protease substrates and discovery of disease biomarkers and therapeutic targets.

Fiber-Type Shifting in Sarcopenia of Old Age: Proteomic Profiling of the Contractile Apparatus of Skeletal Muscles

“…Following the establishment of the concept of the proteome [53] and mass-spectrometrybased proteomics as a highly useful screening tool in the modern biosciences [54], there has been a steady improvement of sample preparation, mass spectrometric instrumentation and data analysis pipelines using both bottom-up [55][56][57] and top-down proteomic techniques [58][59][60]. Importantly, modern biochemical analyses focus on the unifying concept of dynamic proteoforms being the basic units of protein activity [61][62][63]. This has given unprecedented insights into protein diversity and the role of proteins in cellular functions [64], including skeletal muscle tissues [65][66][67][68].…”

Post‐translational modification and phenotype

“…In the second Review article , Wang et al. summarized the available enrichment methods for analyzing protein terminome [5], anothervital molecular diversity associated with protein function and structure. Compared to phosphopeptide enrichment, the efficient separation of protein N‐ and C‐ terminal peptides from a complex mixture is technically more challenging.…”