Table 1.
Typical range of applicability and delivered information from the main NMR methods for the study of protein–ligand interactions.
| NMR methods | Range of applicability | Delivered information | |||||
|---|---|---|---|---|---|---|---|
| K D [M] | Target M W [kDa] | Typical protein/ligand ratio | Labeled target required | Target binding site | Ligand epitope mapping | Ligand selectivity in a mixture | |
| TR‐NOE | 10 −6–10 −3 | no limit | 1:5/1:50 | no | ✓ | ||
| STD NMR | 10 −6–10 −3 | >15 | 1:50/1:200 | no | ✓ | ✓ | |
| waterLogsy | 10 −6–10 −3 | no limit | 1:5/1:50 | no | ✓ | ✓ | |
| diffusion experiments | 10 −6–10 −3 | no limit | 1:1/1:20 | no | ✓ | ✓ | |
| CSP | 10 −9–10 −3 | <100 | 1:1/1:10 | yes | ✓ | ||