DOIAbstract
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, dynamics, activity, and folding of proteins in solution. Peptides and small proteins (<10 kDa) can be studied in detail using 1H NMR and two-dimensional methods including COSY (correlation spectroscopy) and TOCSY (total correlation spectroscopy), which provide 'through-bond' correlations, and NOESY (nuclear Overhauser effect spectroscopy), which provides 'through-space' information. For larger proteins (10-30 kDa), isotope labeling with 15N and 13C is generally required. Resonance assignments are obtained using three-dimensional 15N-edited TOCSY- and NOESY-HSQC or 1H-13C-15N triple-resonance experiments. For proteins larger than ∼30 kDa, high ...
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