6.2 NMR spectroscopy
Nuclear magnetic resonance spectroscopy (NMR) efficiently determines protein molecular structure, function, and folding. The process involves sample preparation and specific measurements to validate structural information. NMR complements X-ray crystallography, particularly for smaller proteins (<30 kDa), and has resolved 17% of Protein Data Bank structures, often when crystallography data is unavailable. Despite being less prominent than X-ray techniques, NMR remains valuable for mapping cofactor binding sites, assessing protein dynamics, detecting different conformations, exploring protein forms, and determining Ionizable group pKa values [64,65].