Resources

Proteomics Databases



Metabolomics Databases

• • Mechanism of Peptidomics Analysis

  Peptidomics analysis is a crucial technique that investigates the composition, structure, and function of specific peptides within protein molecules, thereby revealing the functions and regulatory mechanisms of proteins. Peptides are the building blocks of proteins, and advanced techniques such as mass spectrometry can break down proteins into multiple peptides for further analysis, enabling a comprehensive understanding of the proteins.

• • Application of Peptidomics Analysis

  Peptidomics, the comprehensive analysis of peptides in biological samples using mass spectrometry, plays a crucial role in modern biological research. Peptides are degradation products of proteins and reflect the functional state of proteins within cells. Therefore, peptidomics analysis not only serves as an effective complement to proteomics research but also holds unique value in various biological research fields. Below are the main applications of peptidomics analysis in different domains:

• • Workflow of Peptidomics Analysis

  Proteomics analysis is a systematic approach to studying complex protein mixtures through mass spectrometry (MS). This technique breaks down proteins into smaller peptides for analysis, providing a comprehensive view of the proteome. The workflow of proteomics analysis typically consists of the following steps:

• • Principle of Peptidomics Analysis

  Peptidomics is a significant branch of proteomics, focusing on the study of peptides generated after protein digestion under specific conditions. By detecting and identifying peptides, peptidomics can reveal the structure, function, and post-translational modifications of proteins, thereby assisting researchers in better understanding biological processes within cells.

• • Analysis of N-Glycosylation Sites in Proteins Using PNGase F

  N-glycosylation is a common post-translational modification where sugar chains (glycans) are attached to specific amino acid residues of proteins, altering their function, stability, and structure. N-glycosylation is widespread in cell surface and secreted proteins, playing critical roles in intercellular communication, immune responses, and other biological processes.

• • Quantitative Analysis of N-Glycosylation Sites Based on Isotopic Labeling Mass Spectrometry

  N-glycosylation is a widely occurring form of post-translational modification, playing a vital role in protein folding, quality control, stability, trafficking, and immune responses, thereby impacting various cellular processes. The quantitative analysis of N-glycosylation sites provides insights into the modification levels of proteins, contributing to the understanding of their specific functions in biological mechanisms.

• • Analysis of O-Glycans via Chemical Hydrolysis

  O-glycans are an essential form of glycosylation in glycoproteins, playing crucial roles in regulating cellular communication and immune recognition. Studying the structure and function of O-glycans provides insights into these biological processes. Chemical hydrolysis is a commonly used technique to release and analyze O-glycans from glycoproteins.

• • Analysis of N-Glycan Profiles Using MALDI-TOF-MS

  N-glycans are a crucial modification of glycoproteins on the cell surface, involved in various biological processes such as protein folding, cell-cell communication, and immune response. Accurate analysis of N-glycan structures and compositions is essential for understanding their biological and medical roles. In recent years, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) has become a powerful tool for studying N-glycan profiles

• • Detection of O-Glycans by MALDI-TOF-MS

  O-glycans, a common type of glycosylation modification, are widely present on the surface of proteins and play critical roles in various biological processes such as cell recognition, signal transduction, and immune responses. Due to the structural complexity and high heterogeneity of O-glycans, mass spectrometry-based methods have become indispensable tools for analyzing glycoproteins and studying glycosylation patterns.

• • Detection of Glycosylation Sites and Glycoforms Based on LC-MS/MS

  Glycosylation is a crucial post-translational modification that influences protein folding, stability, and function. Accurate detection of glycosylation sites and glycoforms is essential for studying biological processes, disease mechanisms, and drug development. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has become the primary method for detecting glycosylation sites and glycoforms due to its high sensitivity and resolution.