For proteins that are hard to obtain single crystals because of their high flexibility, NMR spectroscopy is an alternative approach to obtain high-resolution structures.
It can measure the three-dimensional structure of biological macromolecules with atomic resolution under membrane mimetic states or almost physiological environments, especially structural analysis of low-molecular-weight proteins.
It is an appropriate strategy for obtaining information on intermolecular interactions and biomolecular dynamics and for investigating the structure of folded intermediates and the residual structure of unfolded proteins.
Low-transient and low-affinity complexes and small protein-ligand interactions can be studied by NMR spectroscopy.