Double and Triple Resonance Circuits for High-Frequency Probes

Zhang, Q.W.; Zhang, Huiming; Lakshmi, K. V.; Lee, D.K.; Bradley, C. H.; Wittebort, Richard J.

doi:10.1006/jmre.1998.1386

Cited by 32 publications

(23 citation statements)

References 2 publications

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“…With r(O‚‚‚N) distances of 2.777 (GGV) and 2.926 Å (AGG), the NMR data, Table 2, is consistent with this trend. Experience with 15 N DFT calculations also suggests that indirect H bonding to the peptide NH groups could also effect 17 O shielding. To address these possibilities, we compare experiment with DFT calculations, Table 4, of monomeric species and trimer clusters of AGG and GGV constructed from their respective X-ray coordinates.…”

Section: Resultsmentioning

confidence: 99%

“…They stabilize biomolecular structure through hydrogen bonding and mediate dynamic processes such as catalysis and transport of water and ions. Compared to 1 H, 13 C, and 15 N, 17 O chemical shift (CS) dispersion is the largest (∼1500 ppm) of the NMRactive nuclei in protein backbones. In addition, the 17 O experiment reports directly on the electric field gradients from the surrounding electrons and charged groups by way of the quadrupole coupling (QC) interaction.…”

Section: Introductionmentioning

confidence: 99%

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Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors

2006

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Complete 17O chemical shielding (CS) and quadrupole coupling (QC) tensors and their molecular orientations were determined for the central residues in two tripeptides Gly-Gly-Val (GGV) and Ala-Gly-Gly (AGG) by single-crystal NMR methods. Tensor orientations in the two peptides are very similar, however, principal components are different. The most shielded CS and smallest magnitude QC components are normal to the peptide plane, while the most deshielded CS and largest QC components are in the peptide plane either at an angle of 17°(CS) or perpendicular (QC) to the CdO bond. Comparisons of principal components from experiment and DFT calculations indicate that the smaller shielding tensor span in GGV (549 ppm) compared to AGG (606 ppm) is likely due to two factors: a shorter "direct" H-bond distance to the peptide carbonyl oxygen and an "indirect" H bond of the peptide NH to a carboxylate rather than a carbonyl. We anticipate that 17 O NMR should be generally useful for probing H-bonding and local electrostatic interactions in proteins and polypeptides. Using the single-crystal data as an accurate reference, we show that a useful subset of the NMR parameters, QC and CS principal components and their relative orientation, can be obtained with reasonable accuracy from a very high-field (21.2 T), stationary sample powder spectrum.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors

2006

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“…The probe's circuit is based on the design by Cross et al 62 and without an open l/4 line as described by Doty et al 63,64 The high-to low-frequency filter is an LC trap located at the low frequency input. 63,65 The Q of the probe was measured with an empty coil and found to be 180 and 120 on the high-and low-frequency inputs, respectively.…”

Section: Solid-state Nmr Spectroscopymentioning

confidence: 99%

Three-dimensional Structure of the Channel-forming Trans-membrane Domain of Virus Protein “u” (Vpu) from HIV-1

Park

Mrse

Nevzorov

et al. 2003

Journal of Molecular Biology

235

295

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“…The scroll coil is incorporated into the circuit diagrammed in Figure 2, which is an updated version of the original Cross et al (15) circuit and is similar to those used in other applications (16)(17)(18)(19)(20)(21) The circuit is double-tuned to 500 MHz ( 1 H) and 202 MHz ( 31 P). Two variable capacitors (Polyflon NRP/VC10-12-06A, www.polyflon.com) are used in both the 1 H and 31 P tuning networks, indicated as C2 and C3 for the 1 H channel and C6 and C7 for the 31 P channel.…”

Section: Resultsmentioning

confidence: 99%

An efficient 1H/31P double-resonance solid-state NMR probe that utilizes a scroll coil

Grant¹,

Sit²,

Angelis³

et al. 2007

Journal of Magnetic Resonance

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The construction and performance of a scroll coil double-resonance probe for solid-state NMR on stationary samples is described. The advantages of the scroll coil at the high resonance frequencies of 1 H and 31 P include: high efficiency, minimal perturbations of tuning by a wide range of samples, minimal RF sample heating of high dielectric samples of biopolymers in aqueous solution, and excellent RF homogeneity. The incorporation of a cable tie cinch for mechanical stability of the scroll coil is described. Experimental results obtained on a Hunter Killer Peptide 1 (HKP1) interacting with phospholipid bilayers of varying lipid composition demonstrate the capabilities of this probe on lossy aqueous samples.

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Double and Triple Resonance Circuits for High-Frequency Probes

Cited by 32 publications

References 2 publications

Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors

Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors

Three-dimensional Structure of the Channel-forming Trans-membrane Domain of Virus Protein “u” (Vpu) from HIV-1

An efficient 1H/31P double-resonance solid-state NMR probe that utilizes a scroll coil

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Double and Triple Resonance Circuits for High-Frequency Probes

Cited by 32 publications

References 2 publications

Peptide 17O Chemical Shielding and Electric Field Gradient Tensors

Peptide 17O Chemical Shielding and Electric Field Gradient Tensors

Three-dimensional Structure of the Channel-forming Trans-membrane Domain of Virus Protein “u” (Vpu) from HIV-1

An efficient 1H/31P double-resonance solid-state NMR probe that utilizes a scroll coil

Contact Info

Product

Resources

About

Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors

Peptide ¹⁷O Chemical Shielding and Electric Field Gradient Tensors