Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
LeMaster DMdoi
10.1016/0014-5793(88)80452-6subject
Has Abstractpub_date
1988-06-20 00:00:00pages
326-30issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80452-6journal_volume
233pub_type
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