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    Resources

      Proteomics Databases

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      Metabolomics Databases

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    • • What Is Protein Resequencing

      Recombinant protein sequencing is a common technique in biotechnology, which involves the use of biotechnology to sequence proteins, to determine their amino acid sequences. This process typically involves two steps: first, the protein is cut into smaller fragments, and then these fragments are sequenced using mass spectrometry techniques.

    • • Can Mass Spectrometry Detect Protein Sequences?

      Mass spectrometry is a method of substance analysis based on the mass-to-charge ratio of ions. In the mass spectrometer, the sample to be tested is ionized to generate ions, which are then separated according to their mass-to-charge ratio through an electric or magnetic field, and finally, a mass spectrum is generated according to the relative abundance and mass-to-charge ratio of the ions.

    • • Peptide Sequence Determination of Cyclic Peptides

      Cyclic peptides are bioactive substances with a ring-like structure formed by the connection of two or more amino acids through peptide bonds. Cyclic peptides have high structural stability and are not easily hydrolyzed by enzymes. Therefore, they have a very wide range of applications in biology, medicine, chemistry, drug research and development, and other fields. Knowing the peptide sequence of cyclic peptides is a key to understanding its structure and function and developing related drugs.

    • • LC-MS Detection of Host Protein Residues

      Host protein residues are a critical quality control parameter in biopharmaceutical production. Liquid chromatography-mass spectrometry (LC-MS) is a highly effective, highly sensitive, and highly accurate analytical technique, and it is an effective way to study host protein residues.

    • • Peptide Mass Spectrometry Detection Project

      Peptide mass spectrometry is the use of mass spectrometry technology to analyze and detect peptides. Mass spectrometry can be used for molecular weight determination, structural analysis, and isotope abundance determination, etc. The application of peptide mass spectrometry is extensive. It can be used not only to identify unknown peptides but also to perform quantitative analysis on known peptides.

    • • The Relationship Between Protein Interactions and PTMs

      Proteins are the main executors of cellular activities, and their function relies on their precise spatial structure and regulation. Proteins regulate their functions mainly through interactions and post-translational modifications.

    • • Acetylation Modified Proteome

      Protein acetylation is the process by which an acetyl group is covalently attached to lysine residues by enzymatic or non-enzymatic means with acetyl group donors (such as acetyl coenzyme A), which is a very important post-translational modification of proteins.

    • • Proteomics of Macroproteins

      In 1994, Wilkins and Williams first proposed the concept of proteome, which refers to all proteins expressed by cells, tissues, or organisms. In 1997, Peter James further introduced the concept of proteomics, which is the scientific field for studying the proteomes in cells, tissues, or organisms. Proteomics has a wide range of applications, including interpreting genomes, expressing and functioning proteins, and studying protein-protein interactions, etc.

    • • Quantitative Phosphoproteomic Analysis

      It is estimated that about 1/3 of proteins can be phosphorylated at any time in a living organism. Identification of phosphorylated proteins and understanding the dynamics of protein phosphorylation, including the phosphorylation or dephosphorylation of a specific amino acid residue in response to cellular and environmental factors, can help to study the regulation of biological networks at a global level. This emerging field of systems biology is known as phosphoproteomics.

    • • Protein Circular Dichroism Curve Analysis

      Protein is a chiral molecule, with the main photoactive groups originating from the peptide bonds in the peptide chain skeleton, aromatic amino acid residues, and disulfide bridges. When plane circularly polarized light passes through these photoactive chromophores, the photoactive centers absorb the left and right circularly polarized light in the plane circularly polarized light differently, creating a difference in absorption.

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