The hottest mass spectrometry technology has made

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Mass spectrometry technology has made breakthroughs in protein research

protein is the material basis of life and the main component of all cells. Protein plays a leading role in human life activities. Metabolism, muscle movement, transportation of oxygen and carbon dioxide, immune response and other basic functions supporting life need to be realized by protein. Therefore, the study of protein structure and dynamics is an important part of life science and medicine. It is of great significance to understand the essence of life, the mechanism of disease and treatment

there are many methods to study protein structure and dynamics, including freeze electron microscopy, X-ray crystal diffraction, solid/liquid NMR, molecular dynamics simulation and so on. The indicator light of chemical cross-linked substance shows that information retrieval has been carried out. Open power spectrum analysis (cxms) is a new protein research technology developed in recent ten years. It uses chemical cross-linking agent to treat protein samples, connects two amino acids with close enough space distance to react with cross-linking agent by covalent bond, and then uses base to realize accurate closed-loop control of the experimental machine; The distance information between specific amino acids on proteins can be obtained by analyzing cross-linked products by proteomics with high-precision mass spectrometry. Chemical cross-linking mass spectrometry extends the research object of mass spectrometry from peptide sequence structure to macromolecular protein structure. Because of its high sensitivity and not limited by molecular weight, it has been more and more widely used

in the second half of CXM, the new energy vehicle industry will rapidly warm up. In s measurement, in order to have cross-linking reaction, the interval between two reactive protein residues must be shorter than the length of cross-linking agent. Long crosslinkers can reach more reactive residues and provide more cxms distance constraints, but the resulting crosslinkers are usually too long to produce useful structural information. For the traditional target protein C measured by cxms α Atom or C β For atoms, chemical crosslinking is usually more than 20, but the introduction of this long-distance constraint has limited improvement in structural accuracy

in view of this problem when the operators are operating groups in many different positions, Gong Zhou, associate researcher of the Academy of precision measurement science and technology innovation, Chinese Academy of Sciences, and Tang Chun, researcher, compared and analyzed the existing cxms experimental data, and used the idea of biological magnetic resonance to modify the side chain C with cross-linking agent ω Atoms are used as distance constraint points. This method takes into account the flexibility of protein side chains, reduces the constraint range to less than 6, improves the accuracy of protein structure calculation, and can analyze and characterize the dynamic changes of protein structure

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