Broadband homodecoupled NMR spectroscopy with enhanced sensitivity

Sakhaii, Peyman; Haase, Burkhard; Bermel, Wolfgang; Kerssebaum, Rainer; Wagner, Gabriel E.; Zangger, Klaus

doi:10.1016/j.jmr.2013.05.008

Cited by 55 publications

(48 citation statements)

References 13 publications

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“…Hence our comprehensive data set can provide an excellent basis for prediction tools. Also recent advances in the field of off-line hyphenated NMR methods (Jaroszewski, 2005a(Jaroszewski, , 2005b Helge Sakhaii et al, 2013;Zangger & Sterk, 1997), which will allow automated database searches.…”

Section: Discussionmentioning

confidence: 99%

Efficient identification of flavones, flavanones and their glycosides in routine analysis via off-line combination of sensitive NMR and HPLC experiments

et al. 2017

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We present a standardized, straightforward and efficient approach applicable in routine analysis of flavonoids combining sensitive NMR and HPLC experiments. The determination of the relative configuration of sugar moieties usually requires the acquisition of C NMR shift values. We use a combination of HPLC and sensitive NMR experiments (1D-proton, 2D-HSQC) for the unique identification of known flavones, flavanones, flavonols and their glycosides. Owing to their broad range of polarity, we developed HPLC and UHPLC methods (HO/MeOH/MeCN/HCOOH) which we applied and validated by analyzing 46 common flavones and flavanones and exemplified for four plant extracts. A searchable data base is provided with full data comprising complete proton and carbon resonance assignments, expansions of HSQC-spectra, HPLC parameters (retention time, relative retention factor), UV/Vis and mass spectral data of all compounds, which enables a rapid identification and routine analysis of flavones and flavanones from plant extracts and other products in nutrition and food chemistry.

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Section: Discussionmentioning

confidence: 99%

Efficient identification of flavones, flavanones and their glycosides in routine analysis via off-line combination of sensitive NMR and HPLC experiments

et al. 2017

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“…Compared to the recently introduced ZS-decoupling scheme [7], BASH decoupling is less general in that only a subset of the scalar or dipolar interactions can be decoupled. On the other hand, BASH decoupling does not reduce the effective sample volume to a narrow, gradient-selected slice, and therefore observes the same number of spins studied in the regular non-decoupled experiments but with the added benefit of removal of 3 J HH and 1 H- 1 H RDC splittings.…”

Section: Discussionmentioning

confidence: 99%

“…In the indirectly detected t 1 dimension, this typically has been done either by using constant-time evolution [1–3] or, in the case of heteronuclear experiments, by application of a single BIRD pulse unit [4]. Alternatively, a combination of a non-selective 180° pulse and a frequency-selective pulse applied during a static gradient can be used to obtain broadband 1 H- 1 H decoupling [5–7]. This latter method, referred to as Zangger-Sterk or ZS, utilizes the non-selective/selective 180° pulse pair to invert all protons outside of the region inverted by the selective pulse [8].…”

Section: Introductionmentioning

confidence: 99%

“…This particularly elegant method results in dramatic spectral simplification, but again involves a significant cost in sensitivity related to slice selection. In favorable cases, the sensitivity loss can be minimized, however, by rapidly repeating the experiment on adjacent, non-perturbed regions of the sample [7]. For peptides and proteins, frequently much of the interest is focused on detection of amide protons.…”

Section: Introductionmentioning

confidence: 99%

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Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins

Ying

Roche

Bax

2014

Journal of Magnetic Resonance

112

106

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Application of band-selective homonuclear (BASH) 1H decoupling pulses during acquisition of the 1H free induction decay is shown to be an efficient procedure for removal of scalar and residual dipolar couplings between amide and aliphatic protons. BASH decoupling can be applied in both dimensions of a homonuclear 2D NMR experiment and is particularly useful for enhancing spectral resolution in the HN-Hα region of NOESY spectra of peptides and proteins, which contain important information on the backbone torsion angles. The method then also prevents generation of zero quantum and HNz-Hαz terms, thereby facilitating analysis of intraresidue interactions. Application to the NOESY spectrum of a hexapeptide fragment of the intrinsically disordered protein α-synuclein highlights the considerable diffusion anisotropy present in linear peptides. Removal of residual dipolar couplings between HN and aliphatic protons in weakly aligned proteins increases resolution in the 1H-15N HSQC region of the spectrum and allows measurement of RDCs in samples that are relatively strongly aligned. The approach is demonstrated for measurement of RDCs in protonated 15N/13C-enriched ubiquitin, aligned in Pf1, yielding improved fitting to the ubiquitin structure.

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“…Challenges with these methods relate to relatively large Bloch-Siegert shifts, the need to position the side-bands associated with the homonuclear RF gating process outside of the spectral region of interest, and the significant loss in the duty cycle available for actual signal observation. More recently, elegant and effective methods have been introduced which provide broad-band 1 H and, at least in principle, 13 C decoupling by periodically interrupting the FID by combinations of selective and non-selective RF pulses in the presence of pulsed field gradients (Zangger and Sterk 1997; Nilsson and Morris 2007; Meyer and Zangger 2013; Sakhaii et al 2013). When applied in a broad-band manner, this decoupling mode restricts itself to a small volume fraction of the total sample, reducing sensitivity.…”

mentioning

confidence: 99%

13Cα decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins

Ying

Lee

et al. 2014

J Biomol NMR

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Direct detection of 13C can be advantageous when studying uniformly enriched proteins, in particular for paramagnetic proteins or when hydrogen exchange with solvent is fast. A scheme recently introduced for long-observation-window band-selective homonuclear decoupling in solid state NMR, LOW-BASHD (Struppe et al., J. Magn. Reson. 236, 89–94, 2013) is shown to be effective for 13Cα decoupling during direct 13C′ observation in solution NMR experiments too. For this purpose, adjustment of the decoupling pulse parameters and delays is demonstrated to be important for increasing spectral resolution, to reduce three-spin effects, and to decrease the intensity of decoupling side-bands. LOW-BASHD then yields 13C′ line widths comparable to those obtained with the popular IPAP method, while enhancing sensitivity by ca 35%. As a practical application of LOW-BASHD decoupling, requiring quantitative intensity measurement over a wide dynamic range, the impact of lipid binding on the 13C′-detected NCO spectrum of the intrinsically disordered protein α-synuclein is compared with that on the 1H-detected 1H-15N HSQC spectrum. Results confirm that synuclein’s “dark state” behavior is not caused by paramagnetic relaxation or rapid hydrogen exchange.

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Broadband homodecoupled NMR spectroscopy with enhanced sensitivity

Cited by 55 publications

References 13 publications

Efficient identification of flavones, flavanones and their glycosides in routine analysis via off-line combination of sensitive NMR and HPLC experiments

Efficient identification of flavones, flavanones and their glycosides in routine analysis via off-line combination of sensitive NMR and HPLC experiments

Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins

13Cα decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins

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