A Solid-State <sup>17</sup>O Nuclear Magnetic Resonance Study of Nucleic Acid Bases

Wu, Gang; Dong, Shuan; Ida, Ramsey; Reen, Nitin

doi:10.1021/ja011625f

Cited by 128 publications

(220 citation statements)

References 63 publications

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“…The durations of the 90°and selective 180°pulses were given as 4.7 and 18 µs, respectively. (ii) (R28 7 13 R28 7…”

Section: Heteronuclear Dipolar Recouplingmentioning

confidence: 99%

“…Solid-state NMR spectroscopy of 17 O is a powerful tool to study hydrogen bonds since the 17 O chemical shift and quadrupolar coupling are claimed to be very sensitive to the strength and geometry of the hydrogen bonds. In recent years, several groups have demonstrated the feasibility of 17 O NMR experiments in small organic molecules, [3][4][5][6] nucleic acid basis, 7 amino acids, 3,6,[8][9][10] polypeptides, 11,12 and proteins, 13,14 showing a correlation between hydrogen bonding and 17 O chemical shifts and quadrupolar couplings. 17 O is a quadrupolar nucleus (S ) 5 / 2 ) with a low sensitivity and a low natural abundance.…”

Section: Introductionmentioning

confidence: 99%

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Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Brinkmann

Kentgens

2006

J. Phys. Chem. B

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In this contribution we present a comprehensive approach to study hydrogen bonding in biological and biomimetic systems through 17 O and 17 O-1 H solid-state NMR combined with density functional theory calculations of 17 O and 1 H NMR parameters. We explore the signal enhancement of 17 O in L-tyrosine‚HCl using repetitive double-frequency swept radio frequency pulses in solid-state NMR. The technique is compatible with high magnetic fields and fast magic-angle spinning of the sample. A maximum enhancement by a factor of 4.3 is obtained in the signal-to-noise ratio of the selectively excited 17 O central transition in a powdered sample of 17 O η -L-tyrosine‚HCl at an external field of 14.1 T and a spinning frequency of 25 kHz. As little as 128 transients lead to meaningful 17 O spectra of the same sample at an external field of 18.8 T and a spinning frequency of 50 kHz. Furthermore we employed supercycled symmetry-based pulse sequences on the protons to achieve heteronuclear longitudinal two-spin-order (I z S z ) recoupling to determine 17 O-1 H distances. These sequences recouple the heteronuclear dipolar 17 O-1 H couplings, where dipolar truncation is absent, while decoupling the homonuclear proton dipolar interactions. They can be applied at fast magic-angle-spinning frequencies up and beyond 50 kHz and are very robust with respect to 17 O quadrupolar couplings and both 17O and 1 H chemical shift anisotropies, which makes them suitable for the use at high external magnetic fields. The method is demonstrated by determining the 17 O η -1 H distance in L-tyrosine‚HCl at a spinning frequency of 50 kHz and an external field of 18.8 T.

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“…The durations of the 90°and selective 180°pulses were given as 4.7 and 18 µs, respectively. (ii) (R28 7 13 R28 7…”

Section: Heteronuclear Dipolar Recouplingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Brinkmann

Kentgens

2006

J. Phys. Chem. B

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“…19 Recent reports of 17 O NMR from biologically relevant materials have included inorganic molecules interacting with hemeproteins, 10 polypeptides, 11,12 amino acids, 2 and nucleic acid bases. 13 Here, we report the first example of 17 O NMR spectra from a selectively labeled transmembrane peptide, 17 O-[Ala12]-WALP23, as a lyophilized powder and incorporated in hydrated vesicles, opening up new possibilities for applications of 17 O solid-state NMR on real biological systems. WALP23 is a synthetic peptide which represents a consensus sequence for transmembrane protein segments.…”

mentioning

confidence: 99%

Solid-State¹⁷O NMR as a Probe for Structural Studies of Proteins in Biomembranes

et al. 2004

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A key experimental challenge to understand conformational details of membrane proteins is to provide unambiguous atomic-scale information about the molecular bonding arrangement and any changes that occur upon receptor activation. This demands the development of experimental probe techniques to deliver this information of biological and pharmaceutical importance. Solid-state NMR is a nonperturbing approach which can be used to study ligandprotein interactions where molecular size is not limiting and crystallinity is not a requirement. 1 As a first step in addressing this challenge by exploiting 17 O NMR in biomembrane applications, we report here the 17 O solid-state NMR spectra at high field of an 17 O selectively labeled transmembrane peptide in a biomimetic environment.Oxygen plays a key role in the molecular conformation of biopolymers. Among the important information that can be obtained from 17 O, the only NMR-active oxygen isotope, is the isotropic chemical shift (δ iso ), the quadrupolar coupling constant (C Q ), and the asymmetry parameter (η). These parameters are extremely sensitive to the electronic distribution around the nucleus; more specifically, they are sensitive to its protonation state 2 and its involvement in hydrogen bonds. Furthermore, they contain structural information, 2-5 and several methods for determining internuclear distances between oxygen and other nuclei have been developed. 2,6,7 This suggests that oxygen could play a central role in biological NMR studies. However, 17 O has a low natural abundance (0.037%) and a spin (I ) 5 / 2 ) with a corresponding quadrupole interaction that is manifested as significantly broadened signals in NMR spectra. Consequently, 17 O solid-state NMR studies are still relatively uncommon, and selective labeling is essential. Despite these difficulties, in recent years, with the advent of higher magnetic fields and techniques for improving resolution beyond magic angle spinning experiments (MAS), there has been a significant increase in 17 O NMR reports from inorganic materials, such as glasses and zeolites. 8,9 There has been much less 17 O NMR reported from organic materials since 17 O presents even more of a challenge due to the larger quadrupole interaction and, hence, larger line widths. 19 Recent reports of 17 O NMR from biologically relevant materials have included inorganic molecules interacting with hemeproteins, 10 polypeptides, 11,12 amino acids, 2 and nucleic acid bases. 13 Here, we report the first example of 17 O NMR spectra from a selectively labeled transmembrane peptide, 17 O-[Ala12]-WALP23, as a lyophilized powder and incorporated in hydrated vesicles, opening up new possibilities for applications of 17 O solid-state NMR on real biological systems. WALP23 is a synthetic peptide which represents a consensus sequence for transmembrane protein segments. 14 This hydrophobic peptide forms well-defined and wellcharacterized transmembrane R-helices 14 and has special relevance

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“…First, we calculate the contact from oxygen chemisorption on a nano-tube with model semiconductor (5, 0) zigzag and (4, 4) arm chair single-walled carbon nano-tubes (fig 2). Ashrafi et al, 2010;G. Wu, 2002).…”

Section: Introductionmentioning

confidence: 99%

Comparison of NQR of O2, N2 and CO on Surface of Single-Walled Carbon Nanotubes and Chemisorption of Oxygen-Doped on the Surface of Single-Walled Carbon Nanotubes: A DFT and NMR Computational Study

Babanejad¹,

Ашрафи²,

Ghasemi³

et al. 2011

Carbon Nanotubes - Synthesis, Characterization, Applications

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A Solid-State ¹⁷O Nuclear Magnetic Resonance Study of Nucleic Acid Bases

Cited by 128 publications

References 63 publications

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Solid-State¹⁷O NMR as a Probe for Structural Studies of Proteins in Biomembranes

Comparison of NQR of O2, N2 and CO on Surface of Single-Walled Carbon Nanotubes and Chemisorption of Oxygen-Doped on the Surface of Single-Walled Carbon Nanotubes: A DFT and NMR Computational Study

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A Solid-State 17O Nuclear Magnetic Resonance Study of Nucleic Acid Bases

Cited by 128 publications

References 63 publications

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological 17O Solid-State NMR

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological 17O Solid-State NMR

Solid-State17O NMR as a Probe for Structural Studies of Proteins in Biomembranes

Comparison of NQR of O2, N2 and CO on Surface of Single-Walled Carbon Nanotubes and Chemisorption of Oxygen-Doped on the Surface of Single-Walled Carbon Nanotubes: A DFT and NMR Computational Study

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Resources

About

A Solid-State ¹⁷O Nuclear Magnetic Resonance Study of Nucleic Acid Bases

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Sensitivity Enhancement and Heteronuclear Distance Measurements in Biological ¹⁷O Solid-State NMR

Solid-State¹⁷O NMR as a Probe for Structural Studies of Proteins in Biomembranes