Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules

Lars Sonnenberg, Sorin Luca, Marc Baldus

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Chemical-shift-selective (13C, 13C) polarization transfer is analyzed in uniformly labeled biomolecules. It is shown that the spin system dynamics remain sensitive to the distance of interest and can be well reproduced within a quantum-mechanical multiple-spin analysis. These results lead to a general approach on how to describe chemical-shift-selective transfer in uniformly labeled systems. As demonstrated in the case of ubiquitin, this methodology can be used to detect long-range distance constraints in uniformly labeled proteins.

Original languageEnglish (US)
Pages (from-to)100-110
Number of pages11
JournalJournal of Magnetic Resonance
Volume166
Issue number1
DOIs
StatePublished - Jan 1 2004

Fingerprint

Chemical shift
Biomolecules
Ubiquitin
chemical equilibrium
Dynamical systems
Proteins
methodology
Polarization
proteins
polarization

Keywords

  • Distances
  • MAS
  • Polypeptides
  • Solid-state
  • Structure determination

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

Cite this

Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules. / Sonnenberg, Lars; Luca, Sorin; Baldus, Marc.

In: Journal of Magnetic Resonance, Vol. 166, No. 1, 01.01.2004, p. 100-110.

Research output: Contribution to journalArticle

Sonnenberg, Lars ; Luca, Sorin ; Baldus, Marc. / Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules. In: Journal of Magnetic Resonance. 2004 ; Vol. 166, No. 1. pp. 100-110.
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