Protein backbone dynamics through 13C′-13C α cross-relaxation in NMR spectroscopy

Fabien Ferrage, Philippe Pelupessy, David Cowburn, Geoffrey Bodenhausen

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Internal dynamics of proteins are usually characterized by the analysis of 15N relaxation rates that reflect the motions of NHN vectors. It was suggested a decade ago that additional information on backbone motions can be obtained by measuring cross-relaxation rates associated with intra-residue C′Cα vectors. Here we propose a new approach to such measurements, based on the observation of the transfer between two-spin orders 2NzC′z and 2NzC z α. This amounts to "anchoring" the C′z and Cz α operators to the N z term from the amide of the next residue. In combination with symmetrical reconversion, this method greatly reduces various artifacts. The experiment is carried out on human ubiquitin at 284.1 K, where the correlation time is 7.1 ns. The motions of the C′Cα vector appear more restricted than those of the NHN vector.

Original languageEnglish (US)
Pages (from-to)11072-11078
Number of pages7
JournalJournal of the American Chemical Society
Volume128
Issue number34
DOIs
StatePublished - Aug 30 2006

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Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Proteins
Ubiquitin
Amides
Artifacts
Observation
Experiments

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Protein backbone dynamics through 13C′-13C α cross-relaxation in NMR spectroscopy. / Ferrage, Fabien; Pelupessy, Philippe; Cowburn, David; Bodenhausen, Geoffrey.

In: Journal of the American Chemical Society, Vol. 128, No. 34, 30.08.2006, p. 11072-11078.

Research output: Contribution to journalArticle

Ferrage, Fabien ; Pelupessy, Philippe ; Cowburn, David ; Bodenhausen, Geoffrey. / Protein backbone dynamics through 13C′-13C α cross-relaxation in NMR spectroscopy. In: Journal of the American Chemical Society. 2006 ; Vol. 128, No. 34. pp. 11072-11078.
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