A double TROSY hNCAnH experiment for efficient assignment of large and challenging proteins

Dominique P. Frueh, Haribabu Arthanari, Alexander Koglin, Christopher T. Walsh, Gerhard Wagner

Research output: Contribution to journalArticlepeer-review

Abstract

(Figure Presented) We present an experiment that allows for a straightforward assignment of NMR resonances, even in large and/or challenging proteins. A single 3D double-TROSY experiment provides three pairs of sequential correlations between two alpha carbons, two amide protons, and two nitrogen nuclei. Thus, all correlated nuclei can readily be visualized within all dimensions of the resulting spectrum, and chain elongation of sequential amino acids can be effected with this single data set. This resolves ambiguities occurring in traditional methods which involve time-consuming and cumbersome strip comparisons obtained with series of tripleresonance spectra. The experiment makes use of the double TROSY technique to account for signal intensity losses during transfer and evolution periods and was tested on a 500 μM sample of the 33 kDa nonribosomal peptide synthetase protein EntB.

Original languageEnglish (US)
Pages (from-to)12880-12881
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number36
DOIs
StatePublished - Sep 16 2009
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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