Characterization of dynamic processes using deuterium in uniformly 2H,13C,15N enriched peptides by MAS solid-state NMR

Hologne, Maggy; Chen, Zhongjing; Reif, Bernd

doi:10.1016/j.jmr.2005.10.014

Cited by 39 publications

(49 citation statements)

References 79 publications

(101 reference statements)

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“…with angular positions of 0 and γ 0 , jump rate constants k 12 and k 21 , where p 1 = k 21 /(k 12 +k 21 ) and p 2 = k 12 /(k 12 +k 21 ), and a correlation time of τ c = 1/(k 12 +k 21 ) we obtain a correlation function of the form [58,59] (21) which corresponds to a spectral density function of the form (22) For the restricted rotational diffusion in a cone model, the calculation of the correlation function cannot be done analytically in a closed form but only using approximations. The expressions are more complex and can be found in the literature [60].…”

Section: Relaxation In Solidsmentioning

confidence: 99%

“…Spinning sidebands can be fitted to extract tensor parameters, which has been reported for proteins [22]. An experimental challenge comes from the fact that the sideband manifold is very large, and exciting it uniformly requires very large RF field strengths (which are generally not available).…”

Section: Experimental Measurement Of Anisotropic Interactions-mentioning

confidence: 99%

“…In this review we focus on spin-1/2 nuclei, and deliberately omit methods that use quadrupolar couplings, such as deuterium relaxation and line shape analysis. These approaches, (for biomolecules in particular deuterium-based experiments), have been reviewed elsewhere [19][20][21][22][23]. For additional complementary views of (bio-)molecular dynamics studied by solution-or solid-state NMR spectroscopy, we refer the reader to existing reviews [3,5,[23][24][25][26][27][28][29][30]].…”

Section: Introductionmentioning

confidence: 99%

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Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

188

295

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Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR, with an emphasis on the underlying theoretical concepts and differences of MAS solid-state NMR compared to solution-state NMR. The theoretical foundations of nuclear spin relaxation are revisited, focusing on the particularities of spin relaxation in solid samples under magic-angle spinning. We discuss the range of validity of Redfield theory, as well as the inherent multi-exponential behavior of relaxation in solids. Experimental challenges for measuring relaxation parameters in MAS solid-state NMR and a few recently proposed relaxation approaches are discussed, which provide information about time scales and amplitudes of motions ranging from picoseconds to milliseconds. We also discuss the theoretical basis and experimental measurements of anisotropic interactions (chemical-shift anisotropies, dipolar and quadrupolar couplings), which give direct information about the amplitude of motions. The potential of combining relaxation data with such measurements of dynamically-averaged anisotropic interactions is discussed. Although the focus of this review is on the theoretical foundations of dynamics studies rather than their application, we close by discussing a small number of recent dynamics studies, where the dynamic properties of proteins in crystals are compared to those in solution.

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Section: Relaxation In Solidsmentioning

confidence: 99%

Section: Experimental Measurement Of Anisotropic Interactions-mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

188

295

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“…We and others could show previously, that deuteration and back-substitution of exchangeable protons allows for sensitive detection of protons [29][30][31], determination of long range 1 H, 1 H distances [32][33][34], and permits to localize mobile water molecules in the protein structure [35]. In addition, the 2 H spin can be used to probe side chain dynamics [36][37][38][39]. In contrast to the experimental scheme that was suggested by Ramamoorthy et al [40], use of high power decoupling is redundant using the deuteration approach.…”

Section: Introductionmentioning

confidence: 97%

Sensitivity enhancement using paramagnetic relaxation in MAS solid-state NMR of perdeuterated proteins

Linser

Chevelkov

Diehl

et al. 2007

Journal of Magnetic Resonance

Self Cite

127

109

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Previously, Ishii et al., could show that chelated paramagnetic ions can be employed to significantly decrease the recycle delay of a MAS solid-state NMR experiment [N.P. Wickramasinghe, M. Kotecha, A. Samoson, J. Past, Y. Ishii, Sensitivity enhancement in C-13 solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing H-1 T-1 relaxation, J. Magn. Reson. 184 (2007) 350-356]. Application of the method is limited to very robust samples, for which sample stability is not compromised by RF induced heating. In addition, probe integrity might be perturbed in standard MAS PRE experiments due to the use of very short duty cycles. We show that these deleterious effects can be avoided if perdeuterated proteins are employed that have been re-crystallized from D 2 O:H 2 O = 9:1 containing buffer solutions. The experiments are demonstrated using the SH3 domain of chicken a-spectrin as a model system. The labeling scheme allows to record proton detected 1 H, 15 N correlation spectra with very high resolution in the absence of heteronuclear dipolar decoupling. Cu-edta as a doping reagent yields a reduction of the recycle delay by up to a factor of 15. In particular, we find that the 1 H T 1 for the bulk H N magnetization is reduced from 4.4 s to 0.3 s if the Cu-edta concentration is increased from 0 mM to 250 mM. Possible perturbations like chemical shift changes or line broadening due to the paramagnetic chelate complex are minimal. No degradation of our samples was observed in the course of the experiments.

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“…[18,19] [6,20] solange eine induzierte Linienverbreiterung durch Interferenz zwischen der MAS-Frequenz und der Periodizität der Entkopplungssequenz vermieden wird. [20] Die Auflösung in der Protonendimension ist bei der H N -verdünnten Probe eindeutig besser, und ein vollständig aufgelöstes 1 H, 15 N-Korrelationsspektrum kann bereits bei 400 MHz erhalten werden.…”

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Ultrahochaufgelöste ¹H‐MAS‐Festkörper‐NMR‐Spektren unter Verwendung von hohen Deuterierungsgraden

et al. 2006

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Magie? Ein perdeuteriertes Protein, das aus einem 10:90‐Gemisch von H2O und D2O umkristallisiert wurde, weist im MAS‐Festkörper‐NMR‐Spektrum sehr schmale 1HN‐Linienbreiten bei moderaten MAS‐Rotationsfrequenzen auf, ohne dass homo‐ und heteronukleare Entkopplungssequenzen nötig wären. Diese Markierungsstrategie bietet Perspektiven für die Zuordnung von Spinsystemen großer Biomoleküle.

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Characterization of dynamic processes using deuterium in uniformly 2H,13C,15N enriched peptides by MAS solid-state NMR

Cited by 39 publications

References 79 publications

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Sensitivity enhancement using paramagnetic relaxation in MAS solid-state NMR of perdeuterated proteins

Ultrahochaufgelöste ¹H‐MAS‐Festkörper‐NMR‐Spektren unter Verwendung von hohen Deuterierungsgraden

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Characterization of dynamic processes using deuterium in uniformly 2H,13C,15N enriched peptides by MAS solid-state NMR

Cited by 39 publications

References 79 publications

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Sensitivity enhancement using paramagnetic relaxation in MAS solid-state NMR of perdeuterated proteins

Ultrahochaufgelöste 1H‐MAS‐Festkörper‐NMR‐Spektren unter Verwendung von hohen Deuterierungsgraden

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Ultrahochaufgelöste ¹H‐MAS‐Festkörper‐NMR‐Spektren unter Verwendung von hohen Deuterierungsgraden