NMR in structural proteomics and beyond

The contribution of High-resolution NMR to structural proteomics has been reported. NMR spectra are also able to monitor and characterize internal motions of biomolecules occurring over a very broad time range, extending from sub nanoseconds to beyond seconds. The NMR restraints used in structure determination are loose in nature and too few with respect to the degrees of freedom of a protein, to produce a well resolved structure. One possible drawback in protein structural determination by NMR is that the assignment of the NMR signals is still mainly operator- dependent and errors may be possible. The measurement of residual dipolar coupling provides distance- independent structural restraints which, in combination with classical NOE data, have been shown to improve structure determination in multi-domain systems and protein protein or protein ligand complexes. NMR can contribute to cryo-electron microscopy (cryo-EM) investigations of large protein assemblies.