Huang, Z. H., Grape, E. S., Li, J., Inge, A. K. & Zou, X. D. 3D electron diffraction as an important technique for structure elucidation of metal–organic frameworks and covalent organic frameworks. Coord. Chem. Rev. 427, 213583 (2021).
Kuntz, I. D. Structure-based strategies for drug design and discovery. Science 257, 1078–1082 (1992).
Article CAS PubMed Google Scholar
Miller, R. J. D. Femtosecond crystallography with ultrabright electrons and X-rays: capturing chemistry in action. Science 343, 1108–1116 (2014).
Article CAS PubMed Google Scholar
Danelius, E. et al. Solution conformations explain the chameleonic behaviour of macrocyclic drugs. Chem. Eur. J. 26, 5231–5244 (2020).
Article CAS PubMed Google Scholar
Ermondi, G. et al. Managing experimental 3D structures in the beyond-rule-of-5 chemical space: the case of rifampicin. Chem. Eur. J. 27, 10394–10404 (2021).
Article CAS PubMed Google Scholar
Haubrich, K., Spiteri, V. A., Farnaby, W., Sobott, F. & Ciulli, A. Breaking free from the crystal lattice: structural biology in solution to study protein degraders. Curr. Opin. Struct. Biol. 79, 102534 (2023).
Article CAS PubMed Google Scholar
Pradeilles, J. A. et al. Odd–even alternations in helical propensity of a homologous series of hydrocarbons. Nat. Chem. 12, 475–480 (2020).
Article CAS PubMed Google Scholar
Bohle, F. & Grimme, S. Hydrocarbon macrocycle conformer ensembles and 13C-NMR spectra. Angew. Chem. Int. Ed. 61, e202113905 (2022).
Dickman, R. et al. A chemical biology approach to understanding molecular recognition of lipid II by Nisin(1–12): synthesis and NMR ensemble analysis of Nisin(1–12) and analogues. Chem. Eur. J. 25, 14572–14582 (2019).
Article CAS PubMed Google Scholar
Hagele, G. NMR controlled titrations characterizing organophosphorus compounds. Phosphorus Sulfur Silicon Relat. Elem. 194, 361–363 (2019).
Kolmer, A., Edwards, L. J., Kuprov, I. & Thiele, C. M. Conformational analysis of small organic molecules using NOE and RDC data: a discussion of strychnine and α-methylene-γ-butyrolactone. J. Magn. Res. 261, 101–109 (2015).
Navarro-Vázquez, A., Gil, R. R. & Blinov, K. Computer-assisted 3D structure elucidation (CASE-3D) of natural products combining isotropic and anisotropic NMR parameters. J. Nat. Prod. 81, 203–210 (2018).
Peintner, S. & Erdélyi, M. Pushing the limits of characterising a weak halogen bond in solution. Chem. Eur. J. 28, e202103559 (2022).
Article CAS PubMed Google Scholar
Slabber, C. A., Grimmer, C. D. & Robinson, R. S. Solution conformations of curcumin in DMSO. J. Nat. Prod. 79, 2726–2730 (2016).
Article CAS PubMed Google Scholar
Teilum, K., Kunze, M. B., Erlendsson, S. & Kragelund, B. B. (S)Pinning down protein interactions by NMR. Protein Sci. 26, 436–451 (2017).
Article CAS PubMed PubMed Central Google Scholar
Wu, J. et al. Synergy of synthesis, computation and NMR reveals correct baulamycin structures. Nature 547, 436–440 (2017).
Article CAS PubMed Google Scholar
Kwan, E. E. & Huang, S. G. Structural elucidation with NMR spectroscopy: practical strategies for organic chemists. Eur. J. Org. Chem. 2008, 2671–2688 (2008).
Bell, R. A. & Saunders, J. K. Correlation of intramolecular nuclear Overhauser effect with internuclear distance. Can. J. Chem. 48, 1114–1122 (1970).
Overhauser, A. W. Polarization of nuclei in metals. Phys. Rev. 92, 411–415 (1953).
Schirmer, R. E., Noggle, J. H., Davis, J. P. & Hart, P. A. Determination of molecular geometry by quantitative application of nuclear overhauser effect. J. Am. Chem. Soc. 92, 3266–3273 (1970).
Slichter, C. P. The discovery and demonstration of dynamic nuclear polarization — a personal and historical account. Phys. Chem. Chem. Phys. 12, 5741–5751 (2010).
Article CAS PubMed Google Scholar
Karplus, M. Contact electron–spin coupling of nuclear magnetic moments. J. Chem. Phys. 30, 11–15 (1959).
Haasnoot, C. A. G., De Leeuw, F. A. A. M. & Altona, C. The relationship between proton–proton NMR coupling-constants and substituent electronegativities — an empirical generalization of the Karplus equation. Tetrahedron 36, 2783–2792 (1980).
Liu, Y. Z. et al. Application of anisotropic NMR parameters to the confirmation of molecular structure. Nat. Protoc. 14, 217–247 (2019).
Article CAS PubMed Google Scholar
Müntener, T., Joss, D., Häussinger, D. & Hiller, S. Pseudocontact shifts in biomolecular NMR spectroscopy. Chem. Rev. 122, 9422–9467 (2022).
Nitsche, C. & Otting, G. Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags. Prog. Nucl. Magn. Reson. Spectrosc. 98–99, 20–49 (2017).
Pons, M. & Millet, O. Dynamic NMR studies of supramolecular complexes. Prog. Nucl. Magn. Reson. Spectrosc. 38, 267–324 (2001).
Bryant, R. G. The NMR time scale. J. Chem. Educ. 60, 933–935 (1983).
Pearlman, D. A. FINGAR: a new genetic algorithm-based method for fitting NMR data. J. Biomol. NMR 8, 49–66 (1996).
Article CAS PubMed Google Scholar
Wang, J. J., Hodges, R. S. & Sykes, B. D. Generating multiple conformations of flexible peptides in solution based on NMR nuclear Overhauser effect data — application to desmopressin. J. Am. Chem. Soc. 117, 8627–8634 (1995).
Wang, S. et al. Incorporating NOE-derived distances in conformer generation of cyclic peptides with distance geometry. J. Chem. Inf. Model. 62, 472–485 (2022).
Article CAS PubMed Google Scholar
Güntert, P., Braun, W. & Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 517–530 (1991).
Wüthrich, K. NMR of Proteins and Nucleic Acids: 3 (Baker Lecture Series) Vol. 32 (John Wiley & Sons, 1986).
Sattler, M. & Fesik, S. W. Resolving resonance overlap in the NMR spectra of proteins from differential lanthanide-induced shifts. J. Am. Chem. Soc. 119, 7885–7886 (1997).
Speciale, I. et al. Liquid-state NMR spectroscopy for complex carbohydrate structural analysis: a Hitchhiker’s guide. Carbohyd. Polym. 277, 118885 (2022).
Varani, G., Aboulela, F. & Allain, F. H. T. NMR investigation of RNA structure. Prog. Nucl. Magn. Reson. Spectrosc. 29, 51–127 (1996).
Atilaw, Y. et al. Solution conformations shed light on PROTAC cell permeability. ACS Med. Chem. Lett. 12, 107–114 (2021).
Article CAS PubMed Google Scholar
Poongavanam, V. et al. Linker-dependent folding rationalizes PROTAC cell permeability. J. Med. Chem. 65, 13029–13040 (2022).
Article CAS PubMed PubMed Central Google Scholar
Hussain, A., Paukovich, N., Henen, M. A. & Vögeli, B. Advances in the exact nuclear Overhauser effect 2018–2022. Methods 206, 87–98 (2022).
Article CAS PubMed PubMed Central Google Scholar
Vögeli, B. The nuclear Overhauser effect from a quantitative perspective. Prog. Nucl. Magn. Reson. Spectrosc. 78, 1–46 (2014).
Article CAS PubMed Google Scholar
Vögeli, B., Olsson, S., Guntert, P. & Riek, R. The exact NOE as an alternative in ensemble structure determination. Biophys. J. 110, 113–126 (2016). This paper discusses ensemble determination in the context of proteins.
Article CAS PubMed PubMed Central Google Scholar
Keepers, J. W. & James, T. L. A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra. J. Magn. Res. 57,
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