Protein Expression

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Protein Expression

Protein Expression

  • Protein Expression: Application
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Protein Expression NMR (nuclear magnetic resonance)

is a technique used to study the structure and function of proteins at the atomic level. It involves the expression of a protein of interest, purification, and subsequent characterization using NMR spectroscopy.

In protein expression NMR, the protein is expressed in a suitable host organism such as bacteria, yeast, or mammalian cells. The protein is then purified to remove impurities and other proteins. The purified protein is then subjected to NMR spectroscopy, which involves the application of a strong magnetic field to the sample. The interaction of the magnetic field with the nuclei of the protein atoms generates a unique signal that can be used to deduce information about the structure and function of the protein.

Protein expression NMR can provide information on the three-dimensional structure of proteins, protein-ligand interactions, and protein-protein interactions. It can also be used to study protein dynamics, which are important for understanding the function of proteins.

One advantage of protein expression NMR is that it allows for the study of proteins in solution, which more closely mimics the physiological environment of proteins in the body. Additionally, it can be used to study proteins of varying sizes and complexities, from small peptides to large protein complexes.

Overall, protein expression NMR is a powerful technique for studying the structure and function of proteins, and it has many applications in fields such as drug discovery, biotechnology, and structural biology.

References

  1. “Structural basis of nucleosome recognition and modification by MLL methyltransferases” by Antonia Stavropoulos et al., published in Nature in 2016. This paper describes the use of protein expression NMR to determine the structure of the complex between a histone H3 peptide and the SET domain of the MLL1 methyltransferase.
  2. “NMR structure of a complex between the chaperone CbpA and its client protein Ssb” by Boris D. Vögeli et al., published in Nature Structural & Molecular Biology in 2014. This paper describes the use of protein expression NMR to determine the structure of a complex between the chaperone CbpA and its client protein Ssb in solution.
  3. “Structural basis for the recognition of RNA by Ro autoantigen” by Venkat Gopalan et al., published in Nature Structural & Molecular Biology in 2006. This paper describes the use of protein expression NMR to determine the structure of the Ro autoantigen protein in a complex with RNA.
  4. “Structural basis for DNA recognition by FoxO1 and its regulation by posttranslational modification” by Hengrui Liu et al., published in Structure in 2015. This paper describes the use of protein expression NMR to determine the structure of the DNA-binding domain of the FoxO1 transcription factor and its regulation by posttranslational modification.
  5. “Structural basis for the recognition of phosphorylated STAT1 by importin alpha5” by Philip J. Bunker et al., published in Structure in 2017. This paper describes the use of protein expression NMR to determine the structure of the complex between importin alpha5 and phosphorylated STAT1, a key transcription factor involved in immune response.