Mass Spectrometry in Structural Biology

Mass spectrometry (MS) is a powerful analytical technique that has become increasingly important in structural biology. MS is used to determine the mass-to-charge ratio (m/z) of molecules in a sample by ionizing them and then separating the resulting ions based on their mass-to-charge ratio.

In structural biology, MS is often used to determine the mass and composition of proteins, nucleic acids, carbohydrates, lipids, and other biomolecules. This information can then be used to infer the molecular structure and interactions of these molecules.

One of the most important applications of MS in structural biology is the determination of protein structure. MS can be used to determine the molecular mass of intact proteins, which can be used to infer the presence and number of post-translational modifications, such as phosphorylation or glycosylation. MS can also be used to analyze protein fragments generated by enzymatic or chemical cleavage, and this information can be used to identify the amino acid sequence of the protein and to infer its three-dimensional structure.

MS is also useful for analyzing protein-protein interactions and protein-ligand interactions. MS can be used to identify proteins that interact with a given protein, or to identify ligands that bind to a protein of interest. This information can be used to understand the molecular mechanisms underlying protein-protein and protein-ligand interactions, and to design new drugs or other therapeutic agents.

Overall, mass spectrometry has become an important tool in structural biology, providing valuable information about the molecular structure and interactions of biomolecules. The continued development of new MS techniques and instrumentation is likely to lead to even more powerful applications in the future.