In this article, we continue addressing the analysis of ligand-protein interactions by NMR. Now, we will focus on one of the key experiments that monitor the recognition process from the ligand’s viewpoint: 'The Saturation Transfer Difference' method. The employment of this technique permits the existence of interaction and, in favourable cases, the identification of the ligand epitope to be...
In the next issues, we will comment on how to set up different experiments to analyse protein-ligand interactions by using NMR spectroscopy. First, we will focus on experiments that monitor the recognition process from the ligand’s viewpoint, starting with the TRNOESY experiment, which allows the conformation of a particular ligand at the receptor’s binding site to be deduced.
Bruker offers a range of software and hardware that addressses the need for enhanced workflow solutions for NMR spectroscopy research and analysis. These solutions benefit researchers in many disciplines of NMR, while providing productivity enhancements for pharmaceutical users.
JEOL has introduced a probe for NMR analysis of fluorinated compounds prevalent in many new pharmaceutical products.
In this article, Jesús Jiménez Barbero, Scientific Director of CIC bioGUNE, Bizkaia, Spain explains how NMR-based screening is a powerful experimental technique that can be exploited by employing either ligand- or receptor-based methods and illustrates the typical scheme employed when analysing binding from the protein’s point-of-view.