Resources

Proteomics Databases



Metabolomics Databases

• • Application of Peptide Sequencing by Mass Spectrometry

  Mass spectrometry (MS) is a powerful analytical tool widely utilized in proteomics research. Through MS sequencing, scientists can precisely determine the peptide sequences of proteins, uncovering their structure and function. This technology plays a significant role in biological research and clinical diagnostics, especially in protein identification, studying protein-protein interactions, biomarker discovery, and drug development.

• • Mechanism of Peptide Sequencing by Mass Spectrometry

  Mass spectrometry (MS) is a powerful technique in biological research, used to analyze the structure and function of proteins, peptides, nucleic acids, and other biological macromolecules. Through MS, we can determine peptide sequences, which is of great importance in proteomics research.

• • Workflow of Peptide Sequencing by Mass Spectrometry

  Mass spectrometry (MS) sequencing is a powerful tool widely used in proteomics research to analyze and identify the amino acid sequences of proteins.

• • Principle of Peptide Sequencing by Mass Spectrometry

  Mass spectrometry (MS) is a critical analytical technique in contemporary biological research, extensively utilized in proteomics, metabolomics, and clinical diagnostics. Peptide sequencing by mass spectrometry involves detecting and analyzing protein samples with a mass spectrometer to determine their peptide sequences.

• • Advantages and Disadvantages of Peptide Sequencing by Mass Spectrometry

  Mass spectrometry (MS) is an essential analytical tool in modern biological research, widely used in proteomics studies. MS sequencing identifies and quantifies peptide sequences by measuring the mass-to-charge ratio (m/z) of ionized molecules. Despite the numerous advantages of MS sequencing in peptide sequence analysis, it also presents certain challenges and limitations.

• • Protein Phosphorylation Site Detection

  Protein phosphorylation is a core event in cell signal transduction, playing a crucial role in many biological processes, such as cell cycle, proliferation, differentiation, and metabolism. To deeply understand these processes, it is key to determine which proteins are phosphorylated and the precise phosphorylation sites. In recent years, the scientific community has developed a variety of techniques to address this challenge.

• • Common Post-Translational Modifications of Proteins

  Post-translational modification (PTM) refers to the biochemical processes in which amino acid residues in proteins are chemically modified after translation. These chemical modifications greatly expand the functional diversity of proteins, allowing them to participate in various cellular physiological processes.

• • Extinction Coefficient Measurement Method

  The molar extinction coefficient is a unit of measurement that assesses the absorption intensity of a specific wavelength of light by a chemical substance. The molar extinction coefficient of proteins at 280nm is mostly determined by the number of aromatic residues, particularly tryptophan, and can be predicted based on the amino acid sequence. If the molar extinction coefficient is known, it can be used to determine the concentration of protein in a solution.

• • Amino Acid Sequence Determination Methods

  Amino acid sequence determination, also known as protein sequence determination, refers to the process of determining the exact order of amino acid residues in a protein. This information is vital for understanding the structure and function of proteins, identifying new proteins, studying protein interactions, and disease associations.

• • N-Glycosylation Site Analysis

  N-glycosylation is an important protein modification, mainly involving the covalent bond connection between the nitrogen atom of amino acids on proteins and sugar molecules. N-glycosylation typically occurs on the nitrogen atom of asparagine, with the specific sequence pattern being Asn-X-Ser/Thr, where X is any amino acid except proline.