Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered proteins in solution

Bernie O'Hare, Alan J. Benesi, Scott A. Showalter

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Exclusively heteronuclear 13C-detected NMR spectroscopy of proteins in solution has seen resurgence in the past several years. For disordered or unfolded proteins, which tend to have poor 1H-amide chemical shift dispersion, these experiments offer enhanced resolution and the possibility of complete heteronuclear resonance assignment at the cost of leaving the 1H resonances unassigned. Here we report two novel 13C-detected NMR experiments which incorporate a 1H chemical shift evolution period followed by 13C-TOCSY mixing for aliphatic 1H resonance assignment without reliance on 1H detection.

Original languageEnglish (US)
Pages (from-to)354-358
Number of pages5
JournalJournal of Magnetic Resonance
Volume200
Issue number2
DOIs
StatePublished - Oct 1 2009

Fingerprint

Intrinsically Disordered Proteins
Chemical shift
chemical equilibrium
Spectrum Analysis
Chemical Evolution
Spectroscopy
proteins
Protein Unfolding
Amides
spectroscopy
nuclear magnetic resonance
Magnetic Resonance Spectroscopy
amides
Nuclear magnetic resonance spectroscopy
Proteins
Experiments
Nuclear magnetic resonance
Carbon-13 Magnetic Resonance Spectroscopy

All Science Journal Classification (ASJC) codes

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

Cite this

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Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered proteins in solution. / O'Hare, Bernie; Benesi, Alan J.; Showalter, Scott A.

In: Journal of Magnetic Resonance, Vol. 200, No. 2, 01.10.2009, p. 354-358.

Research output: Contribution to journalArticle

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