Paramagnetic relaxation enhancement for protein-observed 19 F NMR as an enabling approach for efficient fragment screening.
| Autor: | Hawk LML; Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN 55455, United States., Gee CT; Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN 55455, United States., Urick AK; Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN 55455, United States.; Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN 46285, United States., Hu H; Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN 46285, United States., Pomerantz WCK; Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN 55455, United States. |
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| Jazyk: | angličtina |
| Zdroj: | RSC advances [RSC Adv] 2016; Vol. 6 (98), pp. 95715-95721. Date of Electronic Publication: 2016 Sep 29. |
| DOI: | 10.1039/C6RA21226C |
| Abstrakt: | Protein-observed 19 F (PrOF) NMR is an emerging tool for ligand discovery. To optimize the efficiency of PrOF NMR experiments, paramagnetic relaxation enhancement through the addition of chelated Ni(II) was used to shorten longitudinal relaxation time without causing significant line broadening. Thus enhancing relaxation time leads to shorter experiments without perturbing the binding of low- or high-affinity ligands. This method allows for time-efficient screening of potential ligands for a wide variety of proteins in the growing field of fragment-based ligand discovery. |
| Databáze: | MEDLINE |
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