Molecular size has limited solution NMR analyses of proteins. We report (C-13C)-C-13 NOESY experiments on a 480 kDa protein, the multi-subunit ferritin nanocage with gated pores. By exploiting C-13-resonance-specific chemical shifts and spin diffusion effects, we identified 75% of the amino acids, with intraresidue C-C connectivities between nuclei separated by 1-4 bonds. These results show the potential of (13)pC-C-13 NOESY for solution studies of molecular assemblies > 100 kDa.
13C-13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin / M.Matzapetakis; P.Turano; E.C.Theil; I.Bertini. - In: JOURNAL OF BIOMOLECULAR NMR. - ISSN 0925-2738. - STAMPA. - 38:(2007), pp. 237-242. [10.1007/s10858-007-9163-9]
13C-13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin
TURANO, PAOLA;BERTINI, IVANO
2007
Abstract
Molecular size has limited solution NMR analyses of proteins. We report (C-13C)-C-13 NOESY experiments on a 480 kDa protein, the multi-subunit ferritin nanocage with gated pores. By exploiting C-13-resonance-specific chemical shifts and spin diffusion effects, we identified 75% of the amino acids, with intraresidue C-C connectivities between nuclei separated by 1-4 bonds. These results show the potential of (13)pC-C-13 NOESY for solution studies of molecular assemblies > 100 kDa.
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