Abstract

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful analytical technique that has transformed the field of structural biology, providing vital insights into the three-dimensional structures and dynamics of biomolecules. This abstract highlights the pivotal role of NMR spectroscopy in elucidating the structures of proteins, nucleic acids, and complex biomolecular assemblies in solution. By exploiting the unique magnetic properties of atomic nuclei, NMR allows researchers to gather detailed information about molecular interactions, conformational changes, and dynamic processes that govern biological functions. Recent advancements in NMR technology, such as higher magnetic field strengths and sophisticated pulse sequences, have further enhanced the sensitivity and resolution of measurements, enabling the study of increasingly complex systems. This review emphasizes how NMR spectroscopy not only aids in understanding the fundamental principles of molecular biology but also supports drug discovery and the design of therapeutic agents by revealing target-ligand interactions. Through the integration of NMR with other structural techniques, researchers are now able to achieve a more comprehensive understanding of biomolecular mechanisms, highlighting NMR spectroscopy's indispensable role in modern structural biology.