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This lecture covers the principles and applications of Nuclear Magnetic Resonance (NMR) spectroscopy in determining protein structures. Starting with the basics of NMR, it explains how atomic nuclei in a magnetic field absorb and re-emit radio waves, providing insights into the chemical environment. The lecture delves into isotope labeling techniques crucial for NMR experiments, emphasizing the importance of 1H-NMR spectra in organic chemistry. It also discusses the role of NMR in medicine, particularly Magnetic Resonance Imaging (MRI). The instructor highlights the significance of NMR restraints in reconstructing protein structures and elucidates the process of converting NMR data into 3D structures. Additionally, the lecture introduces Cryo-Electron Microscopy (Cryo-EM) as a complementary technique to NMR for protein structure determination, showcasing its recent advancements and potential to revolutionize structural biology.