Resources

• • Application of Peptide Structure Determination

  Peptides are molecules formed by the linkage of amino acids through peptide bonds, playing numerous vital biological roles within organisms. Peptides not only constitute hormones, neurotransmitters, enzyme inhibitors, and more, but they also function as signaling molecules, antibiotics, and immune modulators. Therefore, determining peptide structure is essential for understanding their biological functions, developing new drugs, and uncovering biochemical mechanisms.

• • Principle of Peptide Structure Determination

  Peptides are linear molecules composed of amino acids linked by peptide bonds, playing vital roles in numerous biological functions. Determining the structure of peptides is crucial for understanding their functions, as the primary structure (amino acid sequence), secondary structure (local folding), tertiary structure (overall three-dimensional conformation), and quaternary structure (complexes of multiple peptide chains) significantly influence their biological activity.

• • Mechanism of Peptide Identification

  Peptide identification is one of the key steps in modern proteomics research, widely applied in biomedical, drug development, and basic biological studies. At its core, peptide identification relies on mass spectrometry (MS) techniques to accurately identify and quantify peptides, which allows for the deduction of corresponding protein information.

• • Application of Peptide Identification

  Peptide identification is a core technology in proteomics, widely used in protein sequence analysis, structural and functional studies of proteins, and the understanding of various biological processes. With advancements in mass spectrometry, the accuracy and sensitivity of peptide identification have significantly improved, providing an effective means to analyze proteins in complex biological samples.

• • Workflow of Peptide Identification

  Peptide identification is a vital procedure in proteomics research, widely used for protein identification and quantification in biological studies. The workflow encompasses key steps such as sample preparation, enzymatic digestion, peptide separation, mass spectrometry (MS) analysis, and data processing. Each of these steps is essential for ensuring accurate and reproducible results. Below is a refined and more coherent explanation of the peptide identification workflow.

• • Principle of Peptide Identification

  Peptide identification is a critical step in mass spectrometry (MS) analysis and is widely used in proteomics research. Through peptide identification, researchers can identify and quantify proteins in complex biological samples, decipher protein functions, and elucidate their mechanisms of action. Peptide identification typically relies on mass spectrometry technology, particularly tandem mass spectrometry (MS/MS).

• • Label-Free Analysis of Molecular Weight in Recombinant Protein Drugs

  The quality control and molecular weight characterization of recombinant protein drugs are crucial for their safety and efficacy evaluation. In the past, commonly used methods included labeling techniques and mass spectrometry analysis to determine the molecular weight of proteins.

• • Comprehensive TMT Proteomics Analysis of Protein Composition in Biosamples

  Proteomics is the scientific field that studies the overall expression and function of all proteins in an organism. With the continuous development of technology, protein analysis based on tandem mass tagging (TMT) has become an important tool in the field of biological product characterization.

• • Site-Specific Analysis of N-Glycan Modifications Based on MS/MS

  N-glycosylation is a prevalent post-translational modification (PTM) that involves the addition of glycan chains to asparagine residues in proteins. This modification plays a pivotal role in protein folding, stability, and function. Identifying specific N-glycosylation sites is crucial for understanding the biological functions of these modifications.

• • High-Throughput Detection of N-Glycan Modification Sites Using Enzyme-Based Methods

  N-glycosylation is a widespread post-translational modification in eukaryotic organisms, playing a critical role in regulating protein function, signal transduction, protein folding, and stability. N-glycosylation sites are key to many biological processes, including the development of major diseases like cancer and neurodegenerative disorders. Accurately detecting and analyzing N-glycosylation sites is essential for understanding their biological roles.