Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment

Dominique P Frueh, Haribabu Arthanari, Gerhard Wagner

Research output: Contribution to journalArticle

Abstract

An experiment that provides a simple procedure to assign backbone nuclei in proteins is presented. The method relies on time-shared evolution of the coherences present in the (HN)NCAHA and (HA)CANNH experiments. By exploiting the fact that some of the coherences are common to both experiments the alpha and amide protons that are simultaneously detected are correlated with each other and with nitrogen and carbon nuclei. Thus, simultaneous assignment of Hα, HN, Cα and N signals is achieved in a single 3D spectrum. The experiment was tested on the streptococcal protein G B1 domain (GB1) which was easily assigned using a "stairway" procedure and on an 11 kDa domain of the yeast transcriptional co-activator Gal11.

Original languageEnglish (US)
Pages (from-to)187-196
Number of pages10
JournalJournal of Biomolecular NMR
Volume33
Issue number3
DOIs
StatePublished - Nov 2005
Externally publishedYes

Fingerprint

Nuclear magnetic resonance
Proteins
Experiments
Amides
Stairs
Protons
Nitrogen
Carbon
Yeasts
Yeast
Streptococcus IgG Fc-binding protein

Keywords

  • Gal11
  • GB1
  • Nuclear magnetic resonance
  • Protein backbone assignment
  • Time-shared

ASJC Scopus subject areas

  • Spectroscopy
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment. / Frueh, Dominique P; Arthanari, Haribabu; Wagner, Gerhard.

In: Journal of Biomolecular NMR, Vol. 33, No. 3, 11.2005, p. 187-196.

Research output: Contribution to journalArticle

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