View from Nuclear Magnetic Resonance Spectroscopy
Nuclear magnetic resonance (NMR) spectroscopy is one of the three major approaches for determining the structures of biological macromolecules. Historically, NMR spectroscopy was number two after X-ray crystallography in the rate of depositions to the Protein Data Bank (PDB). However, electron cryomicroscopy (CryoEM) recently surpassed NMR in this regard. NMR frequently is used in conjunction with X-ray or CryoEM in structure determinations. NMR has advantages over the other structural approaches in studies of conformational dynamics and interconverting conformational states of proteins and nucleic acids in solution. NMR spectroscopy, itself, can be considered as collection of hybrid methods in that structure determinations rely on the results of several separate magnetic resonance experiments that measure connectivities of magnetic-resonance-active nuclei through covalent bonds or through space or determine relative orientations of magnetic dipoles. NMR results frequently are combined with data from small-angle X-ray scattering or chemical crosslinking in developing structural models. NMR spectroscopy and CryoEM are particularly synergistic in that neither requires crystallization.
KeywordsNMR Spectral assignment Structure determination Data visualization
- Cavanagh J, Fairbrother WJ, Palmer AG, Skelton NJ, Rance M (2010) Protein NMR spectroscopy principles and practiceGoogle Scholar
- Takeuchi K, Frueh DP, Sun ZYJ, Hiller S, Wagner G (2010) CACA-TOCSY with alternate C-13-C-12 labeling: a C-13(alpha) direct detection experiment for main chain resonance assignment, dihedral angle information, and amino acid type identification. J Biomol NMR 47(1):55–63. https://doi.org/10.1007/s10858-010-9410-3 CrossRefGoogle Scholar
- Takeuchi K, Gal M, Takahashi H, Shimada I, Wagner G (2011) HNCA-TOCSY-CANH experiments with alternate 13C- 12C labeling: a set of 3D experiment with unique supra-sequential information for mainchain resonance. J Biomol NMR 49(1):17–26. https://doi.org/10.1007/s10858-010-9456-2 CrossRefPubMedGoogle Scholar
- van Gunsteren WF, Allison JR, Daura X, Dolenc J, Hansen N, Mark AE, Oostenbrink C, Rusu VH, Smith LJ (2016) Deriving structural information from experimentally measured data on biomolecules. Angew Chem Int Ed Engl 55(52):15990–16010. https://doi.org/10.1002/anie.201601828 CrossRefPubMedGoogle Scholar
- Venditti V, Egner TK, Clore GM (2016) Hybrid approaches to structural characterization of conformational ensembles of complex macromolecular systems combining NMR residual dipolar couplings and solution X-ray scattering. Chem Rev 116:6305–6322. https://doi.org/10.1021/acs.chemrev.5b00592 CrossRefPubMedPubMedCentralGoogle Scholar