Untitled

Sørensen, Mads Sølvsten; Meißner, Axel; Sørensen, Ole W.

doi:10.1023/a:1018323913680

Cited by 120 publications

(88 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…19 -21 Figure 1(B) show the basic scheme of an˛/ˇ-HSQC-TOCSY experiment which is based on the so-called spin-state selective excitation (S 3 ) approach. 14,22,23 Two separate 1D spectra are recorded, each one exclusively displaying thę andˇstate of the chosen nitrogen nucleus. This is achieved by only changing the phase of the so-called S 3 pulse and without other extra requirements as additional selective pulses or optimized delays and offsets.…”

Section: Nmr Experimentsmentioning

confidence: 99%

See 1 more Smart Citation

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance

Parella

Belloc

2001

Magnetic Reson in Chemistry

View full text Add to dashboard Cite

Non-selective and selective versions of several proton-detected 1D NMR experiments to be applied to 15 N are proposed. Clean, artifact-free 1D spectra are easily obtained by the effective coherence selection by pulsed-field gradients and the attainable sensitivity is maximized using modern pulse schemes. Despite the low sensitivity inherent to 15 N NMR spectroscopy, the successful application of these experiments is demonstrated for resonance assignments and accurate measurement of both one-bond and long-range proton-nitrogen coupling constants on a model tripeptide at natural abundance.

show abstract

Section: Nmr Experimentsmentioning

confidence: 99%

“…1(B) omitting the TOCSY block]. 14,22,23 When the phase of the so-called S 3 pulse, , is set to x, the conventional in-phase multiplet is achieved [ Fig. 4(B)] with the same sensitivity as in a ge-HSQC spectrum [compare with Fig.…”

Section: (A) (D) 15 N-decoupled Hsqc-pep Spectrum Acquired As In (C)mentioning

confidence: 99%

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance

Parella

Belloc

2001

Magnetic Reson in Chemistry

View full text Add to dashboard Cite

show abstract

“…The J cross talk can be readily removed by taking appropriate linear combinations of the in-phase and antiphase data sets. 11,12,28,30 The amount of cross talk is fairly uniform for different CH spin moieties, facilitating the spectrum processing. For example, use of a scaling factor 0.90 for the in-phase spectrum of the methyl groups, prior to addition and subtraction of the in-phase and antiphase spectrum provided clean separation of individual multiplet components.…”

mentioning

confidence: 99%

SESAME‐HSQC for simultaneous measurement of NH and CH scalar and residual dipolar couplings

Würtz

Permi

2007

Magnetic Reson in Chemistry

View full text Add to dashboard Cite

We present a novel pulse sequence, SESAME-HSQC, for the simultaneous measurement of several NH and CH scalar and residual dipolar couplings in double labeled proteins. The proposed Spin-statE Selective All Multiplicity Edited (SESAME)-HSQC combines gradient selected and sensitivity enhanced (15)N- and constant-time (13)C-HSQC experiments with the recently introduced spin-state selective method (Nolis et al., J. Magn. Reson. 180 (2006) 39-50) for measuring couplings simultaneously at amide and aliphatic regions. Excellent resolution and high sensitivity is warranted by removing all coupling interactions during the indirectly detected t(1) period, and by employing pulsed field gradients for coherence selection and utilizing coherence order selective spin-state selection. The scalar and residual dipolar couplings can be readily measured from a two-dimensional (15)N/(13)C-HSQC spectrum without additional spectral crowding. SESAME-HSQC can be used for epitope mapping by observing chemical shift changes in both amide and aliphatic regions. Simultaneously, potential conversion in protein conformation can be probed by analyzing changes in residual dipolar couplings induced by ligand binding. The pulse sequence is experimentally verified with a sample of (15)N/(13)C enriched human ubiquitin. The internuclear vector directions determined from the residual dipolar couplings are found to be in excellent correlation with those predicted from ubiquitin's refined solution structure.

show abstract

“…In liquid-state NMR, spin-state-selective coherence transfer is obtained using planar mixing or S 3 CT building blocks. 8 Similar J-based spinstate-selective transfer techniques could be envisaged in the solid state. However, schemes using the dipolar coupling may be more appropriate for solid-state applications since most of the (many) existing solid-state dipolar correlation techniques under MAS have a ZQ or DQ average Hamiltonian, and may therefore be used directly for spin-state-selective polarization or coherence transfer.…”

mentioning

confidence: 99%

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

et al. 2003

View full text Add to dashboard Cite

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.

show abstract

Untitled

Cited by 120 publications

References 16 publications

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance

SESAME‐HSQC for simultaneous measurement of NH and CH scalar and residual dipolar couplings

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

Contact Info

Product

Resources

About

Untitled

Cited by 120 publications

References 16 publications

Modern proton‐detected 1D 1H–15N NMR experiments. Application to the measurement of 1H,15N coupling constants at natural abundance

Modern proton‐detected 1D 1H–15N NMR experiments. Application to the measurement of 1H,15N coupling constants at natural abundance

SESAME‐HSQC for simultaneous measurement of NH and CH scalar and residual dipolar couplings

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

Contact Info

Product

Resources

About

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance

Modern proton‐detected 1D ¹H–¹⁵N NMR experiments. Application to the measurement of ¹H,¹⁵N coupling constants at natural abundance