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Protein NMR resonance assignment by isotropic mixing experiments on random fractionally deuterated samples
Author(s) -
LeMaster David M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80452-6
Subject(s) - deuterium , chemistry , isotropy , mixing (physics) , tryptophan , proton , analytical chemistry (journal) , nuclear magnetic resonance , chromatography , atomic physics , physics , amino acid , nuclear physics , biochemistry , quantum mechanics
The 108‐residue protein E. coli thioredoxin has been uniformly enriched to 50% with deuterium at all carbon‐bound hydrogen positions. Isotropic mixing (i.e. TOCSY) experiments have been conducted for both the deuterated and natural‐abundance samples. Using a 54 ms mixing time correlation peaks can be seen for all four protons on the benzenoid ring of tryptophan in both samples. The deuteration results in an average decrease in cross‐sectional area of a factor of 2–3 for the TOCSY cross‐peaks. The cross‐peak intensities for the deuterated sample systematically decrease as a function of the number of protons involved in the transfer process thus overcoming a common ambiguity in the TOCSY experiment.