Paramagnetic relaxation enhancement for protein-observed 19F NMR as an enabling approach for efficient fragment screening

Laura M.L. Hawk, Clifford T. Gee, Andrew K. Urick, Haitao Hu, William C.K. Pomerantz

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Protein-observed 19F (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.

Original languageEnglish (US)
Pages (from-to)95715-95721
Number of pages7
JournalRSC Advances
Volume6
Issue number98
DOIs
StatePublished - 2016

Bibliographical note

Funding Information:
This work was supported by the NSF CAREER award (CHE-1352019) and NIH training grants 5T32GM008347-23 (A. K. U.) and T32-GM08700 (C. T. G.).

Publisher Copyright:
© 2016 The Royal Society of Chemistry.

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