PMC:7594251 / 129329-132613 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7594251","sourcedb":"PMC","sourceid":"7594251","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7594251","text":"Table 3 Advantages and limitations of different NMR techniques developed in recent years.\nNMR Technique Advantages Disadvantages\n1D-NMR Ability to identify simple chemical compounds.High quality resolution and sensitivity for many 1D experiments.Less time consuming compared to 2D NMR. Compared to 2D NMR less details can be obtained for more complex molecules.For nuclei other than 1H and 19F, relative sensitivity is fairly low—requires extra labeling to obtain better spectra.\n2D NMR Ability to identify complex molecules and observe different interactions between the nuclei, e.g., correlations between all spins in one spin system using TOCSY experiment. Requires long times to obtain a proper spectra (up to days).\nUltrafast 2D NMR Greatly reduces time to obtain 2D spectra. Reduced sensitivity.\nSOFAST Significantly reduces acquisition time of HMQC. Relatively low resolution\nNUS Lowers the time of measurement while keeping the same level of resolution. Requires use of reconstruction algorithms since missing data points can lead to artifacts in spectra.\nMDD Multidimensional data are “broken” to one dimensional, which are easier to analyze.Ability to resolve overlapping resonances. Data must be (approximately) symmetrical (Lorentzian shape) to obtain good spectra.\nCS Good reconstruction of weaker peaks. Large computational costs, low performance on noisy data.\nMAX ENT Significant reduction in acquisition time. Nominally Lorentzian peak shapes may be distorted, and peak intensities may be altered.\nIST Greatly reduced time to obtain NMR spectra. Requires a grid of uniformly sampled data points.\nFBDD Often makes stronger binding ligands from weakly binding fragments.Less time and resource intensive. Can be used only for small fragments of compound of interest.\nSAR Direct observation of target binding to ligand. Several types of NMR experiments are possible. Inability to distinguish binding modes, difficult to gage the “true” binding site of ligand to protein.\nSTD Only requires a small amount of sample.Highly reproducible.Allows direct observations of ligand binding. Only works for ligands with low binding affinity (fast chemical exchange). Inability to distinguish binding modes.\nIn cell NMR In vivo studies are possible, can focus on specific cell parts. Special labeling techniques may be required. Spectra may be more challenging to interpret.\nIn silico + NMR Can model protein drug interactions, helps speed up and reduce cost of drug delivery Protein models need to be validated through experimental approach.\nPNMR Can observe proteins interacting with metal ions, long observation distance (10-25 angstroms) between paramagnetic left and nearby atoms. Paramagnetic left required in the system.\nALARM NMR Elimination of false positives from HTS methods It requires synthesis of human La antigen protein.\nssNMR Enables the characterization of a chemical compound in a solid-state form such as a tablet/pill.Provides insight into the physical properties of a compound. Significant broadening of the spectral lineshapes due to anisotropic spin interactions.\nRelaxation editing Noticeable difference in spectra of binding and non-binding ligands. Sets the lower limit of time for which experiments can be 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