1H‐Observe 1H2H Dipolar Recoupling by REDOR and Rotary Resonance Recoupling

Karki, Ichhuk; Mihaliuk, Eugene; Gullion, Terry

doi:10.1002/ijch.201300098

Cited by 3 publications

(1 citation statement)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reduction in sensitivity can be mitigated by introducing protons in random locations, which also has the advantage of providing relatively isolated protons for measurement of long-range distance restraints [11]. In sparsely protonated samples, heteronuclear dipolar couplings between 1 H and 2 H nuclei can also be measured [12]. For nanocrystalline samples, the resolution in the 1 H dimension of multidimensional solid-state spectra is sufficiently high to allow chemical shift assignments, as demonstrated for proteins such as ubiquitin [13,14], the SH3 domain [8], and GB1 [15].…”

Section: Introductionmentioning

confidence: 99%

Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules

Collier

Sengupta

Espinosa

et al. 2017

Journal of Magnetic Resonance

View full text Add to dashboard Cite

Extensive deuteration is frequently used in solid-state NMR studies of biomolecules because it dramatically reduces both homonuclear (H-H) and heteronuclear (H-C and H-N) dipolar interactions. This approach greatly improves resolution, enables low-power rf decoupling, and facilitates H-detected experiments even in rigid solids at moderate MAS rates. However, the resolution enhancement is obtained at some cost due the reduced abundance of protons available for polarization transfer. Although deuterium is a useful spin-1 NMR nucleus, in typical experiments the deuterons are not directly utilized because the available probes are usually triple-tuned to H,C and N. Here we describe aH/C/H/N MAS ssNMR probe designed for solid-state NMR of extensively deuterated biomolecules. The probe utilizes coaxial coils, with a modified Alderman-Grant resonator for the H channel, and a multiply resonant solenoid forC/H/N. A coaxial tuning-tube design is used for all four channels in order to efficiently utilize the constrained physical space available inside the magnet bore. Isolation among the channels is likewise achieved using short, adjustable transmission line elements. We present benchmarks illustrating the tuning of each channel and isolation among them and the magnetic field profiles at each frequency of interest. Finally, representative NMR data are shown demonstrating the performance of both the detection and decoupling circuits.

show abstract

Section: Introductionmentioning

confidence: 99%

Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules

Collier

Sengupta

Espinosa

et al. 2017

Journal of Magnetic Resonance

View full text Add to dashboard Cite

show abstract

Description of an rf field-strength controller for solid-state NMR experiments

Lusk

Gullion

2018

Solid State Nuclear Magnetic Resonance

View full text Add to dashboard Cite

Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences

Zhang

et al. 2016

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

Experimental characterization of one-bond heteronuclear dipolar couplings is essential for structural and dynamics characterization of molecules by solid-state NMR. Accurate measurement of heteronuclear dipolar tensor parameters in magic angle spinning NMR requires that the recoupling sequences efficiently reintroduce the desired heteronuclear dipolar coupling term, fully suppress other interactions (such as chemical shift anisotropy and homonuclear dipolar couplings), and be insensitive to experimental imperfections, such as radio frequency (rf) field mismatch. In this study, we demonstrate that the introduction of window delays into the basic elements of a PARS sequence results in a greatly improved protocol, termed windowed PARS (wPARS), which yields clean dipolar lineshapes that are unaffected by other spin interactions and are largely insensitive to experimental imperfections. Higher dipolar scaling factor can be attained in this technique with respect to PARS, which is particularly useful for the measurement of relatively small dipolar couplings. The advantages of wPARS are verified experimentally on model molecules N-Acetyl-Valine (NAV) and a tripeptide Met-Leu-Phe (MLF). The incorporation of wPARS into 3D heteronuclear correlation experiments permits accurate site-specific determination of dipolar tensors in proteins, as demonstrated on dynein light chain 8 (LC8). Through 3D wPARS recoupling based spectroscopy we have determined both backbone and sidechain dipolar tensors in LC8 in a residue-resolved manner. We discuss these in the context of conformational dynamics of LC8. We have addressed the effect of paramagnetic relaxant Cu(II)-EDTA doping on the dipolar coupling parameters in LC8 and observed no significant differences with respect to the neat sample permitting fast data collection. Our results indicate that wPARS is advantageous with respect to the windowless version of the sequence and is applicable to a broad range of systems including but not limited to biomolecules.

show abstract

¹H‐Observe ¹H²H Dipolar Recoupling by REDOR and Rotary Resonance Recoupling

Cited by 3 publications

References 34 publications

Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules

Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules

Description of an rf field-strength controller for solid-state NMR experiments

Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences

Contact Info

Product

Resources

About