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An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple
M Ikura1, M Krinks, D A Torchia
1Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD 20892.
FEBS Letters
|June 18, 1990
Abstract:
By simultaneously incorporating in a protein 13C-carbonyl- and 15N-labeled amino acids with different levels of enrichment, characteristics asymmetric doublet-like patterns are observed for 15N nuclei that are directly adjacent to the 13C1-labeled residues, providing unambiguous identification of a large number of unique dipeptide fragments of the protein. Additional assignments and qualitative structural information can be obtained from such a selectively labeled protein by recording multiple bond correlation spectra. The procedure is demonstrated for the protein calmodulin, complexed with calcium.