Homonuclear broadband-decoupled absorption spectra, with linewidths which are independent of the transverse relaxation rate

Bax, Ad; Mehlkopf, A.F.; Smidt, J.

doi:10.1016/0022-2364(79)90088-x

Cited by 89 publications

(72 citation statements)

References 4 publications

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“…A "pure shift" spectrum, without multiplets, would bring a resolution improvement to match that achieved in signal-to-noise ratio (SNR). Such spectra can be obtained, [1][2][3][4][5][6][7][8][9][10][11][12][13] but until recently have been very little used, for a variety of reasons including lack of generality, insensitivity, nonlinearity, and complexity. Here we show that second-generation pure shift methods are eminently practical for complex chemical systems, giving resolution equivalent to spectrometers of several GHz with mm sensitivity.…”

mentioning

confidence: 99%

Pure Shift ¹H NMR: A Resolution of the Resolution Problem?

Faulkner²,

et al. 2010

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mentioning

confidence: 99%

Pure Shift ¹H NMR: A Resolution of the Resolution Problem?

Faulkner²,

et al. 2010

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“…The assignments of IP-COSY for peptides can be facilitated from the observation of 4 J(HN,HB) and 4 J(HD,HB) (for tyrosine) connectivities. 3 J(H,H) coupling constants of larger than 4 Hz in the fingerprint region of peptides can be directly derived from the separation of doublets. For oligonucleotides of moderate size, the complete network of sugar protons of DNA was observed owing to increased sensitivity in IP-COSY, but cross peaks relating to RNA sugar protons were weak.…”

Section: Resultsmentioning

confidence: 99%

“…In (B) and (C), T c D T m D 13 ms and T c D 0.1 ð 16/ns ms. The coupling constants, 3 J, as measured are given next to the peaks. In these spectra, the various ratios (R S/N ) of the S/N of IP-COSY or CT-COSY versus DQF-COSY can be measured.…”

Section: J(hh) Measurementsmentioning

confidence: 99%

“…14,22 Another scheme to achieve in-phase coherence detection uses the constant time evolution mode. 3,4 CT-COSY was shown to be more sensitive than DQF-COSY and permits direct measurement of J(H,H) and residual dipolar coupling without isotope enrichment. 14,15,20,21 This experiment utilizes a CT parameter T c to maximize the magnetization transfer at all t 1 increments and eliminates J-modulation in the F 1 dimension.…”

Section: Introductionmentioning

confidence: 99%

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IP-COSY, a totally in-phase and sensitive COSY experiment

et al. 2005

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The IP-COSY experiment presented in this paper gives an in-phase spectral presentation in both the F(1) and F(2) dimensions by a combined use of a constant evolution time (CT) in t(1) and a symmetrical refocusing period before t(2). Compared with DQF-COSY and CT-COSY, IP-COSY further alleviates the effect of signal reduction due to a small ratio p (= J/linewidth), showing (1) improved lineshape and cross-peak definition and (2) especially enhancement in signals of the peaks of small active J coupling constant and the peaks of broader linewidth. A new strategy was adopted to eliminate or reduce effectively artifactual peaks by adding a 0.1-0.2 ms variation to the time delays of the CT period used for each scan of the FID in IP-COSY and CT-COSY. (3)J(H,H) coupling constants of larger than 4 Hz in the fingerprint region of peptides can be directly derived from the separation of doublets. IP-COSY cross peaks are stronger than those in DQF-COSY by 4-20-fold for tested peptides and oligonucleotides (MW < 8 kDa) with acquisition and processing parameters used in the work, and they are easier to identify than those in CT-COSY. The overall improvement in IP-COSY should make the detection/autodetection of the COSY cross peaks and the measurements of the various coupling constants more easily achieved, providing valuable information for the structure elucidation of peptides/small proteins and oligonucleotides.

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“…12 PDSD then yields spin-state-selective CO->C α polarization transfer. During the PDSD mixing period, CO polarization (I z ) is transferred to C α polarization (S z ) by the dipolar coupling, but the two-spin order 2I z S z , present after t 1 evolution, is not affected by the dipolar coupling.…”

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confidence: 99%

Resolution Enhancement in Multidimensional Solid-State NMR Spectroscopy of Proteins Using Spin-State Selection

et al. 2003

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We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer techniques. The selection and transfer of single states allow the removal of the J-coupling contribution from the line width in both the direct and indirect spectral dimensions. This is demonstrated with a new spin-state-selective CO−Cα correlation experiment, applied to a microcrystalline 85-residue protein. With this new sequence, all four components of the CO−Cα cross-peaks are separated into different spectra, obtained by linear combination of four recorded data sets. Line narrowing of up to 44% was obtained on the protein sample for the spin-state-selective CO−Cα spectrum compared to a standard spin-diffusion experiment. The new technique also allows an easy distinction between “direct” and “relayed” transfer cross-peaks.

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Homonuclear broadband-decoupled absorption spectra, with linewidths which are independent of the transverse relaxation rate

Cited by 89 publications

References 4 publications

Pure Shift ¹H NMR: A Resolution of the Resolution Problem?

Pure Shift ¹H NMR: A Resolution of the Resolution Problem?

IP-COSY, a totally in-phase and sensitive COSY experiment

Resolution Enhancement in Multidimensional Solid-State NMR Spectroscopy of Proteins Using Spin-State Selection

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Homonuclear broadband-decoupled absorption spectra, with linewidths which are independent of the transverse relaxation rate

Cited by 89 publications

References 4 publications

Pure Shift 1H NMR: A Resolution of the Resolution Problem?

Pure Shift 1H NMR: A Resolution of the Resolution Problem?

IP-COSY, a totally in-phase and sensitive COSY experiment

Resolution Enhancement in Multidimensional Solid-State NMR Spectroscopy of Proteins Using Spin-State Selection

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Product

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Pure Shift ¹H NMR: A Resolution of the Resolution Problem?

Pure Shift ¹H NMR: A Resolution of the Resolution Problem?