Author: Matzapetakis Manolis Turano Paola Theil Elizabeth Bertini Ivano
Publisher: Springer Publishing Company
ISSN: 0925-2738
Source: Journal of Biomolecular NMR, Vol.38, Iss.3, 2007-07, pp. : 237-242
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Abstract
Molecular size has limited solution NMR analyses of proteins. We report 13C–13C NOESY experiments on a 480 kDa protein, the multi-subunit ferritin nanocage with gated pores. By exploiting 13C-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 13C–13C NOESY for solution studies of molecular assemblies >100 kDa.
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