13C- 13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin

Molecular size has limited solution NMR analyses of proteins. We report (13)C-(13)C NOESY experiments on a 480 kDa protein, the multi-subunit ferritin nanocage with gated pores. By exploiting (13)C-resonance-specific chemical shifts and spin diffusion effects, we identified 75% of the amino acids, w...

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Bibliographic Details
Published in:Journal of biomolecular NMR 2007-07, Vol.38 (3), p.237-242
Main Authors: Matzapetakis, Manolis, Turano, Paola, Theil, Elizabeth C, Bertini, Ivano
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - chemistry
Animals
Carbon - analysis
Carbon - chemistry
Carbon Isotopes
Ferritins - chemistry
Molecular Weight
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Structure, Secondary
Rana catesbeiana
Solutions
Time Factors
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Summary:Molecular size has limited solution NMR analyses of proteins. We report (13)C-(13)C NOESY experiments on a 480 kDa protein, the multi-subunit ferritin nanocage with gated pores. By exploiting (13)C-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)C-(13)C NOESY for solution studies of molecular assemblies >100 kDa.
ISSN:0925-2738
1573-5001
DOI:10.1007/s10858-007-9163-9