Low concentration of a Gd-chelate increases the signal-to-noise ratio in fast pulsing BEST experiments

Sibille, Nathalie; Bellot, Gaëtan; Wang, Jing; Déméné, Hélène

doi:10.1016/j.jmr.2012.07.022

Cited by 4 publications

(3 citation statements)

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“…The use of alternative uncharged Gd(III) probes such as Gd 2 (L 7 )(H 2 O) 2 , Gd(DO3A) , and Gd(HP-DO3A) , as well as complexes with increasing charge, such as [Gd(EDTA)] 1– , [Gd(DTPA)] 2– , and [Gd(DOTP)] 5− , has also been explored (Figure ). The strong PRE effects generated by Gd(III) complexes have also proven useful to shorten the T 1 relaxation time of H 2 O and protein protons without greatly increasing the line widths of protein NMR signals, enabling sensitivity enhancements by faster scan repetition rates. It is important to note, however, that some proteins may harbor specific binding sites for some of these complexes, which can be made apparent by PCSs generated by complexes with paramagnetic lanthanoid ions other than Gd(III).…”

Section: General Overview Of Natural and Chemically Generated Paramag...mentioning

confidence: 99%

“…355 Gd(DO3A), and Gd(HP-DO3A), 356 as well as complexes with increasing charge, such as [Gd(EDTA)] 1− , 357 [Gd(DTPA)] 2− , 358 and [Gd(DOTP)] 5− , 359 has also been explored (Figure 13). The strong PRE effects generated by Gd(III) complexes have also proven useful to shorten the T 1 relaxation time of H 2 O 360 and protein protons 361 without greatly increasing the line widths of protein NMR signals, enabling sensitivity enhancements by faster scan repetition rates.…”

Section: Chemicalmentioning

confidence: 99%

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Paramagnetic Chemical Probes for Studying Biological Macromolecules

et al. 2022

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Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent years witnessed a great increase in the variety of probes for the study of biological macromolecules (proteins, nucleic acids, and oligosaccharides). This Review aims to provide a comprehensive overview of the existing paramagnetic chemical probes, including chemical synthetic approaches, functional properties, and selected applications. Recent developments have seen, in particular, a rapid expansion of the range of lanthanoid probes with anisotropic magnetic susceptibilities for the generation of structural restraints based on residual dipolar couplings and pseudocontact shifts in solution and solid state NMR spectroscopy, mostly for protein studies. Also many new isotropic paramagnetic probes, suitable for NMR measurements of paramagnetic relaxation enhancements, as well as EPR spectroscopic studies (in particular double resonance techniques) have been developed and employed to investigate biological macromolecules. Notwithstanding the large number of reported probes, only few have found broad application and further development of probes for dedicated applications is foreseen.

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Section: General Overview Of Natural and Chemically Generated Paramag...mentioning

confidence: 99%

Section: Chemicalmentioning

confidence: 99%

Paramagnetic Chemical Probes for Studying Biological Macromolecules

et al. 2022

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“…It has been previously shown that labile backbone amides may gain additional sensitivity in BEST‐based sequences such as SOFAST‐HMQC, because of their chemical exchange with the solvent water . This additional sensitivity gain may be further improved in the presence of paramagnetic agents …”

Section: Introductionmentioning

confidence: 99%

Nutation frequency modulation on NMR signal of nuclear spins in chemical exchange with solvent water under the BEST conditions

Yao

Keizer

2014

Magnetic Reson in Chemistry

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Solvent exchange properties of protein backbone amide protons provide valuable residue-specific information on protein solvent accessibility, structure stability and flexibility and hence are of significant interest in structural biology. NMR has served as a unique means for the characterization of chemical exchange including proton amide exchange with solvent water at residue-specific levels across a broad range of exchange rates. One of the methods used for the characterization of protein backbone amide exchange by NMR involves the use of progressive selective irradiation of the water resonance. Here, we report the experimental observation of the nutation frequency (strength of RF field used for the irradiation of water resonance) modulation on amide proton signals for those in exchange with the solvent water under the band-selective excitation short transient (BEST) conditions. Compared with conventional saturation transfer of water magnetization experiments, this nutation frequency modulation observed on signal of nuclear spins under the BEST conditions potentially offers a quick identification of protein backbone amides in rapid exchange with solvent water.

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