Review Article
Biophysical Approaches Facilitate Computational Drug Discovery for ATP-Binding Cassette Proteins
Table 2
Comparison of commonly used biophysical techniques.
| Parameter | Biophysical technique | X-ray crystallography | NMR spectroscopy | Cryo-EM |
| MW range of proteins | 2–3,000 kDa | 60–65 kDa for all-atom; 800–1,000 kDa with sparse labeling | 2–3,000 kDa | Time required | Up to several years | Up to 1 year | A few months | Typical resolution range | 2–4 Å | N/A | >4 Å | Membrane proteins | Y | Y | Y | Protein dynamics | N | Y | N | Recapitulates physiology | N | Y/N | Y | Artifacts | Crystallization artifacts, single conformation | Reflecting conformational averaging | Possible sample preparation artifacts | Expertise required | Y | Y | Y | Major advantage | Streamlined, high resolution information | Providing information on protein dynamics | Fully functional macromolecular complexes | Major disadvantage | Requiring stable protein crystal that diffracts well | Requiring high concentration sample | Low signal-to-noise ratio for proteins smaller than 300 kDa |
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