Interference effects in the relaxation of a pair of unlike nuclei

Goldman, M.

doi:10.1016/0022-2364(84)90055-6

Cited by 223 publications

(251 citation statements)

References 14 publications

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“…The system exhibits relatively long T 2 times for 1 H and 15 N which is reflected in high spectral resolution. The average differential line broadening [45] of 15 N was around 10 Hz, as determined for 16 well-resolved residues in the HN 2D spectrum recorded on the 850 MHz spectrometer at an MAS rate of 20 kHz without HN J decoupling in the 15 N dimension. This value is close to previously reported ones for microcrystalline samples [10,13], and does not advocate TROSY-type techniques [23,46,47] for mild resolution improvement at the cost of significant sensitivity losses.…”

Section: High-resolution Proton-detected Spectra Of Deuterated Prgi Nmentioning

confidence: 86%

Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins

Chevelkov

Habenstein

Loquet

et al. 2014

Journal of Magnetic Resonance

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a b s t r a c tProton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained at a low protonation level of 10-20% at exchangeable amide positions. We developed efficient experimental protocols for resonance assignment tailored for this system and the employed experimental conditions. Using exclusively dipolar-based interspin magnetization transfers, we recorded two sets of 3D spectra allowing for an almost complete backbone resonance assignment of the needle subunit PrgI. The additional information provided by the well-resolved proton dimension revealed the presence of two sets of resonances in the N-terminal helix of PrgI, while in previous studies employing 13 C detection only a single set of resonances was observed.

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Section: High-resolution Proton-detected Spectra Of Deuterated Prgi Nmentioning

confidence: 86%

Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins

Chevelkov

Habenstein

Loquet

et al. 2014

Journal of Magnetic Resonance

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“…For instance, if the interaction tensors have favourable relative orientations, the fluctuations of dipole-dipole interactions and anisotropic chemical shifts can partially cancel each other, a phenomenon which is used in Transverse Relaxation Optimised SpectroscopY (TROSY) [7][8][9][10][11]. Similar kinds of interferences between several dipolar interactions can also be observed in methyl groups [12].…”

Section: Introductionmentioning

confidence: 99%

Long-lived coherences for line-narrowing in high-field NMR

Sarkar¹,

Ahuja²,

Vasos³

et al. 2011

Progress in Nuclear Magnetic Resonance Spectroscopy

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“…Thus Eq. (2) evolves under fast relaxation as the sum of λ and η to: (3) Here Ω N represents a chemical shift offset in radians/s and J is the N-H spin coupling in Hz. Then the composite inversion pulse flips the proton spin state from β to α and, thus, converts the upfield magnetization to downfield magnetization.…”

Section: Pulse Sequence Designmentioning

confidence: 99%

“…Anytime that multiple spin relaxation interactions are modulated by the same motion, or highly correlated motions, the possibility of cross-correlation contributions to spin relaxation arises [3]. Although these effects sometimes represent a complication that needs to be carefully eliminated [4], they can be used to advantage in many situations.…”

Section: Introductionmentioning

confidence: 99%

Direct measurement of dipole–dipole/CSA cross-correlated relaxation by a constant-time experiment

Liu

Prestegard

2008

Journal of Magnetic Resonance

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Relaxation rates in NMR are usually measured by intensity modulation as a function of a relaxation delay during which the relaxation mechanism of interest is effective. Other mechanisms are often suppressed during the relaxation delay by pulse sequences which eliminate their effects, or cancel their effects when two data sets with appropriate combinations of relaxation rate effects are added. Cross-correlated relaxation (CCR) involving dipole-dipole and CSA interactions differ from autocorrelated relaxation (ACR) in that the signs of contributions can be changed by inverting the state of one spin involved in the dipole-dipole interaction. This property has been exploited previously using CPMG sequences to refocus CCR while ACR evolves. Here we report a new pulse scheme that instead eliminates intensity modulation by ACR and thus allows direct measurement of CCR. The sequence uses a constant time relaxation period for which the contribution of ACR does not change. An inversion pulse is applied at various points in the sequence to effect a decay that depends on CCR only. A 2-D experiment is also described in which chemical shift evolution in the indirect dimension can share the same constant period. This improves sensitivity by avoiding the addition of a separate indirect dimension acquisition time. We illustrate the measurement of residue specific CCR rates on the non-myristoylated yeast ARF1 protein and compare the results to those obtained following the conventional method of measuring the decay rates of the slow and fast-relaxing 15 N doublets. The performances of the two methods are also quantitatively evaluated by simulation. The analysis shows that the shared constant-time CCR (SCT-CCR) method significantly improves sensitivity.

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Interference effects in the relaxation of a pair of unlike nuclei

Cited by 223 publications

References 14 publications

Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins

Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins

Long-lived coherences for line-narrowing in high-field NMR

Direct measurement of dipole–dipole/CSA cross-correlated relaxation by a constant-time experiment

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