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].