Resources

Proteomics Databases



Metabolomics Databases

• • Mechanism of Protein Deamidation and Its Impact on Function

  Protein deamidation is the process in which the amide groups of asparagine (Asn) or glutamine (Gln) residues within a protein are hydrolyzed, resulting in the formation of aspartic acid (Asp) or glutamic acid (Glu). This process is widespread in living organisms and has profound effects on the structure and function of proteins.

• • Application of Protein Deamidation in Disease Mechanism Studies

  Protein deamidation is a crucial post-translational modification process that plays a vital role in various biological activities. Deamidation refers to the conversion of asparagine or glutamine residues in proteins from an amide group to a carboxyl group, leading to structural alterations and functional regulation. This process is essential for maintaining cellular function, signal transduction, and protein degradation, and is closely linked to the onset and progression of multiple diseases.

• • Workflow of Protein Deamidation Analysis via Mass Spectrometry

  Protein deacetylation is a pivotal post-translational modification (PTM) that plays an essential role in modulating protein function, stability, and interactions. The evolution of mass spectrometry (MS) technology has made MS-based protein deacetylation analysis a fundamental tool in this area of study.

• • Principle of Protein Deamidation Analysis

  Protein post-translational modifications (PTMs) are crucial mechanisms that regulate protein functionality and structural diversity. Among these, deamidation refers to the conversion of asparagine (Asn) or glutamine (Gln) residues into aspartic acid (Asp) or glutamic acid (Glu), respectively. This modification alters protein structure and stability, and it is closely associated with the development of various diseases, making its precise analysis critically important.

• • How Many Proteins Can Be Sequenced in Proteomics?

  Protein sequencing is a high-throughput technique that helps us understand the composition and function of proteins. It involves analyzing proteins in biological samples to determine their sequences and expression levels. This information is crucial for unraveling the mysteries of life and understanding various biological processes and disease mechanisms.

• • Guidelines for Optimizing Efficient Protein Mass Spectrometry Identification

  Protein mass spectrometry identification is a key technique in the field of biomedicine, providing a powerful tool for unraveling the mysteries of biomolecules. By analyzing the mass spectrometry data of proteins, we can understand their structure, function, and interactions, providing valuable information for drug development, disease diagnosis, and basic research.

• • Exploring Peptide Structure Identification: Mass Spectrometry

  Peptides are biopolymers composed of amino acids, and the identification of their higher-order structure is crucial for understanding their function and interactions. In the field of biopharmaceuticals, accurate determination of the higher-order structure of peptide drugs is required for their development and optimization.

• • SILAC-Based Co-IP-MS for High-Throughput Protein Interaction Analysis

  Protein-protein interactions (PPIs) are a crucial area of biological research, essential for understanding complex cellular processes. Studying how proteins interact with other molecules can reveal their roles in processes such as signal transduction, metabolism, and gene expression regulation.

• • Peptide Sequencing Applications: Breakthrough in Protein Structure Characterization

  Protein is one of the fundamental functional molecules in living organisms, and its structure is closely related to its function. Understanding the structure of proteins is of great significance for revealing their functions and studying related diseases. Peptide sequencing, as a key technique, provides a breakthrough for the characterization of protein structures.

• • SILAC-Based Protein-Protein Interaction Analysis Using Mass Spectrometry

  Protein-Protein Interactions (PPIs) are a critical area of biological research, essential for almost all cellular processes and functions. Understanding these interactions not only elucidates fundamental biological mechanisms but also identifies potential therapeutic targets for diseases. In recent years, mass spectrometry (MS)-based methods for analyzing PPIs have gained widespread use, particularly when combined with Stable Isotope Labeling by Amino acids in Cell culture (SILAC) technology.