Abstract

Nuclear Magnetic Resonance (NMR) spectroscopy has emerged as a powerful and versatile tool in drug discovery, offering unique insights into the structure, dynamics, and interactions of biomolecules at atomic resolution. This abstract explores the various applications of NMR spectroscopy in drug discovery, including ligand screening, protein-ligand binding studies, and fragment-based drug design. NMR-based methods such as chemical shift mapping, relaxation analysis, and diffusion measurements provide detailed information on the binding kinetics, thermodynamics, and conformational changes associated with protein-ligand interactions, facilitating the identification of lead compounds and optimization of drug candidates. Moreover, NMR spectroscopy allows for the characterization of protein dynamics and allosteric regulation, providing valuable mechanistic insights into drug-target interactions. Additionally, recent advancements in NMR technology, such as high-throughput screening methods and the development of selective isotope labeling techniques, have further expanded the capabilities of NMR in drug discovery. Overall, harnessing the power of NMR spectroscopy holds great promise for accelerating the drug discovery process and driving innovation in pharmaceutical research.