Rotating-Frame Overhauser Transfer via Long-Lived Coherences

Teleanu, Florin; Topor, Alexandru; Serafin, Diana; Sadet, Aude; Vasos, Paul R.

doi:10.3390/sym13091685

Cited by 4 publications

(7 citation statements)

References 24 publications

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“…LLC's have an oscillatory evolution (𝜈 𝐿𝐿𝐶 = 𝐽 𝐼𝑆 ) and the recorded 1D spectra consist of a superposition of in-phase and anti-phase peaks depending on the mixing period 𝜏 𝑚𝑖𝑥 . The oscillating transfer from glycine-based LLC's to neighbouring spins with a frequency equal to the scalar coupling (𝜈 𝐿𝐿𝐶 = 𝐽 𝐼𝑆 ) is dampened by relaxation as molecular tumbling slows down 35 . Calculations indicate that oscillations of observed signals stemming from the magnetisation source are quenched both by relaxation and by small oscillations at the transfer site K, induced by local couplings (see Supporting Information).…”

Section: Long-lived Coherencesmentioning

confidence: 99%

Improved detection of magnetic interactions in proteins based on long-lived coherences

Sadet,

Ianc,

Teleanu

et al. 2024

Preprint

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Living systems rely on molecular building blocks with low structural symmetry. Therefore, the constituent amino-acids and nucleotides yield short-lived nuclear magnetic responses to electromagnetic radiation. Magnetic signals are at the basis of molecular imaging, structure determination and interaction studies in the liquid state. Interactions between magnetic nuclei can only be detected provided the lifetimes of spin order are sufficient. In J-coupled pairs of nuclei, long-lived coherences (LLC’s) can be excited between states with different spin-permutation symmetry. In solution state, as the molecular weight of analytes increases, coherences with long lifetimes are needed to yield advantageous through-space magnetisation transfers. In protein Lysozyme, weighing 14.3 kDa, we sustained coherences with lifetimes twice as long as those of classical magnetisation for the aliphatic protons of glycine residues. We found that, in this protein of significant molecular weight, LLC’s yield substantial through-space magnetisation transfers: in agreement with theory, spin-order transfer stemming from LLC’s overcame transfers from classical coherences by factors 2-3. Furthermore, the permutation symmetry of LLC-based transfers allowed mapping the positions of interacting atoms in the protein structure with respect to the molecular plane of glycine residues in a stereospecific manner. These findings can extend the scope of liquid-state high-resolution spectroscopy in the analysis of biomolecular complexes of high molecular weight.

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Section: Long-lived Coherencesmentioning

confidence: 99%

Improved detection of magnetic interactions in proteins based on long-lived coherences

Sadet,

Ianc,

Teleanu

et al. 2024

Preprint

Self Cite

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“…The sensitivity of LLC's to the presence of nearby nuclei yields new information compared to classical coherences. The interaction of an LLC superposition with a neighboring spin has been described both theoretically and via experiments for small-molecule systems (7). The dependence on the effective correlation time modulating the interaction, c, of the transfer of magnetisation from LLC to a neighbour situated at a distance of 4 Å from the average position of Gly-H 2,3 is compared to the classical transfer of transverse magnetisation in Figure 1B.…”

Section: Long-lived Coherencesmentioning

confidence: 99%

“…The transfer from Gly protons to neighbours is oscillating in the fastdiffusion limit and the oscillations are dampened by relaxation in the slow diffusion limit. (7) The intensity of observed transfers in Lysozyme is affected by the different components of the overall tumbling of the protein and local anisotropic motions. This sets effective local correlation times for each glycine interaction.…”

Section: Magnetisation Transfer In 1d and 2d Llc-roe Build-upsmentioning

confidence: 99%

“…This opened the way for recording 1 H magnetic resonance transitions with relaxation time constants extended by up to a factor 9, even in peptides or proteins, namely for Gly protons. However, lifetime enhancements for magnetic transitions were only detected experimentally for small molecules and there remained the challenge of demonstrating that such long-lived coherences can be used for magnetization transfer in a protein, though theoretically this has been deemed possible (7). We demonstrate herein that 1H-based LLC's with lifetimes twice as long as standard coherences, TLLC > 2T2, can be observed in 14 kDa protein Lysozyme and used to transfer magnetisation to remote amino-acids within the protein fold, thereby establishing distance constraints.…”

Section: Introductionmentioning

confidence: 99%

“…Transitions between nuclear singlet and triplet configurations were first observed as low-frequency oscillations in low magnetic fields (4). In high magnetic fields, these transitions offer extended time-frames for Overhauser-type transfer in the rotating frame (6)(7)(8) featuring, in high-resolution NMR magnets, decays up to 9 times slower than those of standard NMR transitions. LLC's can be sustained with various methods in 2D experiments affording resolution at moderate amplitudes of the sustaining field (17).…”

Section: Introductionmentioning

confidence: 99%

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Long-lived coherences for magnetic interactions in proteins

Teleanu,

Ciumeica,

Ianc

et al. 2023

Preprint

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Living systems rely on molecular building blocks of low symmetry such as amino-acids and nucleotides, which generally yield short-lived magnetic transitions in response to electromagnetic radiation. This is the first demonstration that in proteins of relatively large size local magnetic symmetry can be induced to enable the detection of interactions based on long–lived coherent transitions of nuclear spins. Long–lived coherences (LLC′s) are superpositions of quantum states with singlet and triplet spin–permutation symmetries that feature significantly longer relaxation time constants compared to those of standard nuclear spin coherences. We report in this study that glycine residues in Lysozyme, a 14.3 kDa protein, feature LLC′s with relaxation time constants twice as long as the classical counterparts. Using a new excitation method for LLC′s, Lysozyme Gly–Hα; dipolar interactions with neighboring hydrogen spins were mapped in a high magnetic field – at 950 MHz 1H Larmor frequency – for glycine residues 4, 49, 54, 67, 117, and 126. As predicted by theory, the positions of nearby atoms in the protein structure on one side or the other of the reflection plane containing the C2 axes of rotation for Gly–Hα2,3atom pairs determine the signs of magnetic interaction signals. LLC–based transfers yield stereospecific signals from glycine residues to 1H neighboring atoms. The symmetry–encoded sign of the detected signals provides angle constraints, in addition to the distance information. LLC probes based on naturally–abundant1H spins can be useful for in–cell spectroscopy, circumventing the introduction of heterogenous spin labels for following protein–ligand or protein–protein interactions in the natural environment. This is the first demonstration that magnetisation transfer through space from long–lived coherences can be obtained in proteins. Applications of LLC′s were believed to be limited to systems featuring fast rotational motion in solution, mainly small molecules. This new LLC–based method yields stereospecific distance constraints and has the potential to extend the protein–size domain for the study of intra– and intermolecular interactions.

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Improved detection of magnetic interactions in proteins based on long-lived coherences

Ianc,

Teleanu,

Ciumeică

et al. 2024

Commun Chem

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Living systems rely on molecular building blocks with low structural symmetry. Therefore, constituent amino acids and nucleotides yield short-lived nuclear magnetic responses to electromagnetic radiation. Magnetic signals are at the basis of molecular imaging, structure determination and interaction studies. In solution state, as the molecular weight of analytes increases, coherences with long lifetimes are needed to yield advantageous through-space magnetisation transfers. Interactions between magnetic nuclei can only be detected provided the lifetimes of spin order are sufficient. In J-coupled pairs of nuclei, long-lived coherences (LLC’s) connect states with different spin-permutation symmetry. Here in, we show sustained LLC’s in protein Lysozyme, weighing 14.3 kDa, with lifetimes twice as long as those of classical magnetisation for the aliphatic protons of glycine residues. We found for the first time that, in a protein of significant molecular weight, LLC’s yield substantial through-space magnetisation transfers: spin-order transfer stemming from LLC’s overcame transfers from classical coherences by factors > 2. Furthermore, in agreement with theory, the permutation symmetry of LLC-based transfers allows mapping interacting atoms in the protein structure with respect to the molecular plane of glycine residues in a stereospecific manner. These findings can extend the scope of liquid-state high-resolution biomolecular spectroscopy.

show abstract

Rotating-Frame Overhauser Transfer via Long-Lived Coherences

Cited by 4 publications

References 24 publications

Improved detection of magnetic interactions in proteins based on long-lived coherences

Improved detection of magnetic interactions in proteins based on long-lived coherences

Long-lived coherences for magnetic interactions in proteins

Improved detection of magnetic interactions in proteins based on long-lived coherences

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