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

doi:10.1016/j.jmr.2009.07.014

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 journal › Article › peer-review

35 Scopus citations

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 language	English (US)
Pages (from-to)	354-358
Number of pages	5
Journal	Journal of Magnetic Resonance
Volume	200
Issue number	2
DOIs	https://doi.org/10.1016/j.jmr.2009.07.014
State	Published - Oct 2009

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Nuclear and High Energy Physics
Condensed Matter Physics

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10.1016/j.jmr.2009.07.014

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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.",

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AU - Benesi, Alan J.

AU - Showalter, Scott A.

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AB - 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.

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

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