An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
FEBS Lett. 1990 Jun 18;266(1-2):155-8
Authors: Ikura M, Krinks M, Torchia DA, Bax A
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.
PMID: 2114317 [PubMed - indexed for MEDLINE]
Source:
PubMed