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NMR spectroscopy provides structural information about biomolecules at the atomic level in aqueous solution. While the analysis of the structures of folded proteins is one main application of protein NMR spectroscopy, the method also offers unique possibilities to investigate the dynamics of such defined folds. Thereby, we can observe structural changes in response to binding events and map out interaction interfaces. In Integrative Structural Biology approaches, NMR spectroscopy is often used in combination with X-ray crystallography, electron microscopy or other structure-sensitive analytical techniques and computational methods.
- Discuss the possibilities offered by NMR spectroscopy for the analysis of the 3D atomic structures of biological macromolecules and the limitations of the methods. Specifically consider the amount of sample needed, the degree of sample purity, sample preparation requirements, molecular mass of the target biomolecule/complex, time requirements, cost of required equipment and possibilities to assess structural dynamics.
- What kind of NMR-experiment would you propose to observe changes in the folding process of a protein with and without post-translational modification?
- Compare NMR spectroscopy with other techniques used for structure analysis, such as X-ray crystallography, single-particle cryo-electron microscopy or crosslinking/mass spectrometry.
- You are interested in a protein that consists of a small and a large domain. You want to find out, if both domains are flexibly connected and thus tumble largely independently of each other in solution, or if these two domains interact with each other. What sort of NMR experiment would you perform to investigate a possible interaction?
- Discuss the role of structural biological approaches in the drug development process.