Aug 2026· International Journal of Molecular Sciences· Vol 27· 0 citations· 64 references
Medicine
TL;DR
How NMR experiments characterize molecular recognition in protein–ligand interactions is discussed, which enables a workflow that accelerates the progression from initial binding identification to structural and dynamic characterization.
Abstract
Protein–ligand interactions are fundamental to physiological processes and drug discovery. Based on the types of information on protein–ligand interactions provided by nuclear magnetic resonance (NMR) experiments, these NMR experiments can be categorized into three distinct classes: (i) molecular-level qualitative binding detection, (ii) residue-level mapping of binding interfaces, and (iii) atomic-level structure determination and conformational dynamics of protein–ligand complexes. This hierarchy enables a workflow that accelerates the progression from initial binding identification to structural and dynamic characterization. In this review, we discuss how these experiments characterize molecular recognition. Notably, the term “ligand” in this article refers exclusively to small molecules.
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