- Samples for NMR are 'free' in solution and data recorded at a wide range of conditions (including temperatures) yet give residue-specific (atomic) resolution, making it ideal for titrations and studies of dynamic processes.
- It is highly complementary to X-ray crystallography and cryoEM because the NMR signal generally increases (rather than decreases) with increasing dynamics.
- Recent advances in how data is acquired mean that even complex 3D datasets can be recorded in minutes to hours, and sample requirements for concentration and labelling are lowered (see Sample Requirements).
NMR's ability to investigate conformationally flexible regions in proteins is increasingly important with the shift in attention in structural biology from static structures to conformational changes and interactions. In the AlphaFold
era, the access to accurate structural models for any protein makes residue-specific NMR data mapping much more powerful. In addition, NMR is relatively tolerant to structural and chemical heterogeneity, making it a powerful screening tool.
The most common uses of NMR include:
- Quantitative and site-specific information for interactions. NMR can provide binding site locations and any conformational changes occurring upon binding. The binding events can be protein-protein, protein-ligand, protein-nucleic acid, etc.
- Small molecule screens
- Identifying and quantifying flexibility in proteins, including timescale and magnitude. The flexibility might be extensive (IDPs) or localised.
- Diagnostics to evaluate sample condition and homogeneity (structural and chemical).
NMR can provide a wide range of information. A more detailed list is on the What can you do? page.
