Published Research - Department of Chemistry

 

Date of this Version

2015

Citation

J Biomol NMR. 2015 September ; 63(1): 53–58. doi:10.1007/s10858-015-9962-3.

Comments

Copyright 2015 The Authors.

Abstract

NMR ligand-affinity screens are vital to drug discovery, are routinely used to screen fragment-based libraries, and used to verify chemical leads from high-throughput assays and virtual screens. NMR ligand-affinity screens are also a highly informative first step towards identifying functional epitopes of unknown proteins, as well as elucidating the biochemical functions of protein-ligand interaction at their binding interfaces. While simple one-dimensional (1D) 1H NMR experiments are capable of indicating binding through a change in ligand line shape, they are plagued by broad, ill-defined background signals from protein 1H resonances. We present an uncomplicated method for subtraction of protein background in high-throughput ligand-based affinity screens, and show that its performance is maximized when phase-scatter correction (PSC) is applied prior to subtraction.

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