The correlation between hydrogen-bond lengths and proton chemical shifts in crystals

Jeffrey, G. A.; Yeon, Younghee

doi:10.1107/s0108768186098038

Cited by 151 publications

(167 citation statements)

References 8 publications

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“…These changes are consistent with a lengthening of the first hydrogen bond by deuteration (due to the shortened O-D covalent bond) and a shortening of the adjacent hydrogen bond in response [shorter hydrogen bonds give rise to increased chemical shifts (26)], as depicted schematically in Fig. 3A.…”

Section: Direct Detection Of Physical Coupling Between the Tyr-42 Andsupporting

confidence: 61%

“…Indeed, elongation of the O-H bond of Glu-46 was observed in a recent 1.5 Å resolution neutron structure of PYP (24). Proton migration decreases sigma bond electron density around the bridging proton and deshields it relative to other protons, resulting in a more downfield NMR chemical shift that correlates with the O⅐⅐⅐O, O-H, and H⅐⅐⅐O distances of the hydrogen bond (25,26).…”

mentioning

confidence: 99%

“…As discussed above, a more downfield chemical shift for a hydrogen-bonded proton correlates with greater proton migration away from the donor oxygen and a shorter donor-acceptor O⅐⅐⅐O distance in small molecules (26). On the basis of these small-molecule correlations, the chemical shifts of the downfield peaks in PYP may be used to estimate O⅐⅐⅐O distances of 2.56 and 2.61 Å for the hydrogen bonds donated by Glu-46 and Tyr-42, respectively.…”

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confidence: 99%

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Hydrogen bond dynamics in the active site of photoactive yellow protein

Sigala

Tsuchida

Herschlag

2009

Proc. Natl. Acad. Sci. U.S.A.

145

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Hydrogen bonds play major roles in biological structure and function. Nonetheless, hydrogen-bonded protons are not typically observed by X-ray crystallography, and most structural studies provide limited insight into the conformational plasticity of individual hydrogen bonds or the dynamical coupling present within hydrogen bond networks. We report the NMR detection of the hydrogen-bonded protons donated by Tyr-42 and Glu-46 to the chromophore oxygen in the active site of the bacterial photoreceptor, photoactive yellow protein (PYP). We have used the NMR resonances for these hydrogen bonds to probe their conformational properties and ability to rearrange in response to nearby electronic perturbation. The detection of geometric isotope effects transmitted between the Tyr-42 and Glu-46 hydrogen bonds provides strong evidence for robust coupling of their equilibrium conformations. Incorporation of a modified chromophore containing an electron-withdrawing cyano group to delocalize negative charge from the chromophore oxygen, analogous to the electronic rearrangement detected upon photon absorption, results in a lengthening of the Tyr-42 and Glu-46 hydrogen bonds and an attenuated hydrogen bond coupling. The results herein elucidate fundamental properties of hydrogen bonds within the complex environment of a protein interior. Furthermore, the robust conformational coupling and plasticity of hydrogen bonds observed in the PYP active site may facilitate the larger-scale dynamical coupling and signal transduction inherent to the biological function that PYP has evolved to carry out and may provide a model for other coupled dynamic systems.charge delocalization ͉ hydrogen bond coupling ͉ protein structure ͉ signal transduction

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Section: Direct Detection Of Physical Coupling Between the Tyr-42 Andsupporting

confidence: 61%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Hydrogen bond dynamics in the active site of photoactive yellow protein

Sigala

Tsuchida

Herschlag

2009

Proc. Natl. Acad. Sci. U.S.A.

145

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“…The combination of X-ray or neutron crystallography with NMR spectroscopy is a promising future area of crystallographic research (cf. Etter, 1989;Etter, Hoge & Vojta, 1988;Jeffrey & Yeon, 1986;Harris, 1988).…”

Section: Introductionmentioning

confidence: 99%

Crystallographic studies of carbohydrates

Jeffrey¹

1990

Acta Crystallogr B Struct Sci

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151

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The monosaccharides which constitute the monomer units of many important industrial and biological macromolecules are well represented among the 2000 crystal structures of the carbohydrate class 45 of the Cambridge Structural Database. There are few examples of crystal structure analyses of the corresponding acids, but many of their calcium salts and calcium salt complexes. With the exception of the disaccharides and cyclodextrins, the oligosaccharides are not well represented, with less than ten trisaccharides, one tetrasaccharide and one hexasaccharide-iodide complex. Two important conformational factors are the Hassel-Ottar effect and the anomeric effect, both of which have been studied using crystallographic data. Hydrogen bonding is ubiquitous in carbohydrate crystals and generally involves all the hydroxyls as both donors and acceptors, and some of the ring and glycosidic oxygens as acceptors. These hydrogen bonds tend to form finite or infinite chains. In hydrates, these chains are linked through the water molecules to form networks. Cyclic hydrogen-bond systems are observed in the cyclodextrins. Long-chain alkylated carbohydrates provide a large class of thermotropic and lyotropic liquid crystals, and some non-ionic surfactants which have been shown to be useful for membrane-protein solubilization and crystallization.

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“…Ab initio calculations [9] suggested that the origin of this effect is the deshielding of the principal component of the 1 H shift tensor perpendicular to the hydrogen bond as the bond length decreases. Subsequently, a linear correlation between the isotropic 1 H shift δiso( 1 H) and d(H…O) was established by comparison with neutron diffraction data [10]. Many similar relationships have been found for phosphates [11], hydrosilicates [12], selenites [13] and amino acids [14], and these are commonly used to extract hydrogen bond lengths from solid-state NMR measurements.…”

Section: Introductionmentioning

confidence: 99%

1 H CSA parameters by ultrafast MAS NMR: Measurement and applications to structure refinement

Miah

Cresswell

Iuga

et al. 2017

Solid State Nuclear Magnetic Resonance

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A 1 H anisotropic-isotropic chemical shift correlation experiment which employs symmetry-based recoupling sequences to reintroduce the chemical shift anisotropy in ν1 and ultrafast MAS to resolve 1 H sites in ν2 is described. This experiment is used to measure 1 H shift parameters for L-ascorbic acid, a compound with a relatively complex hydrogen-bonding network in the solid. The 1 H CSAs of hydrogen-bonded sites with resolved isotropic shifts can be extracted directly from the recoupled lineshapes. In combination with DFT calculations, hydrogen positions in crystal structures obtained from X-ray and neutron diffraction are refined by comparison with simulations of the full two-dimensional NMR spectrum. The improved resolution afforded by the second dimension allows even unresolved hydrogen-bonded sites 1 H to be assigned and their shift parameters to be obtained.

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The correlation between hydrogen-bond lengths and proton chemical shifts in crystals

Cited by 151 publications

References 8 publications

Hydrogen bond dynamics in the active site of photoactive yellow protein

Hydrogen bond dynamics in the active site of photoactive yellow protein

Crystallographic studies of carbohydrates

1 H CSA parameters by ultrafast MAS NMR: Measurement and applications to structure refinement

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