Protein NMR resonance assignment by isotropic mixing experiments on random fractionally deuterated samples.

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 Lett

journal_title

FEBS letters

authors

LeMaster DM

doi

10.1016/0014-5793(88)80452-6

subject

Has Abstract

pub_date

1988-06-20 00:00:00

pages

326-30

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)80452-6

journal_volume

233

pub_type

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