Ligand–Protein Binding and Screening Using NMR Spectroscopy
 

Ligand–Protein Binding and Screening Using NMR Spectroscopy

Publication date: 2017
Source:Encyclopedia of Spectroscopy and Spectrometry</br>
Author(s): Bridget A. Becker</br>
Investigating protein–ligand binding using NMR spectroscopy can provide insights into the protein-binding pocket, the contacts the ligand makes with the protein, the bound ligand conformation, and the binding constant. Methods to investigate protein-ligand binding by NMR are divided into two categories: ligand-detected experiments, including diffusion, STD, NOESY, and relaxation experiments, and protein-detected experiments (usually called target-detected experiments), which involve following perturbations of the protein resonance chemical shifts in the presence and absence of ligand. Screening using NMR spectroscopy cannot match in speed and limit of detection screening by high-throughput screening (HTS), but the information content from protein–ligand binding and screening experiments by NMR can be greater, and much weaker binding can be detected. Therein lies the advantage of screening a generally smaller and more tightly focused library of compounds by NMR techniques as compared to HTS screens.
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