Double quantum filters are used to filter out single quantum magnetization and allow the passage of double quantum magnetization. In the proton observe heteronuclear case, the double quantum filter (like the BIRD filter) allows the selective observation of the weak satellite signals from protons coupled to dilute spin I = 1/2 X nuclei (e.g. X = 13C, 15N, 29Si ....) but rejects the strong singlets from the uncoupled protons in the vicinity of 12C, self decoupled 14N, and 28Si . The figure below illustrates the heteronuclear double quantum filter described by Stefan Berger and Siegmar Braun in 200 and More NMR Experiments applied to the 1H NMR spectrum of tetramethylsilane. The bottom trace of the figure shows a conventional 1H NMR spectrum. The middle trace was collected using a 1H-29Si double quantum filter and shows only the 1H-29Si doublet. The top trace was collected using a 1H-13C double quantum filter and show only the 1H-13C doublet. In both cases there is excellent suppression of the 1H singlet signal.
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Abstract Here we describe phasing anomalies observed in gradient sensitivity enhanced 15N-1H HSQC spectra, and analyze their origin. It is shown that, as a result of 15N off-resonance effects, dispersive contributions to the 1H signal become detectable, and lead to 15N-offset dependent phase errors. Strategies that effectively suppress these artifacts are presented.
Content Type Journal Article
Category Article
Pages 199-207
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[CNS Yahoo group] Double protonated His side chains have charge +1 independent of pH
Double protonated His side chains have charge +1 independent of pH
Hi all, I am using ccpn/aria/cns combination for my structural work. I discovered a probably bad fact during the aria/cns structure calculation. In the ccpn
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[NMR paper] Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
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Annu Rev Phys Chem. 2003;54:531-71
Authors: Drobny GP, Long JR, Karlsson T, Shaw W, Popham J, Oyler N, Bower P, Stringer J, Gregory D, Mehta M, Stayton PS
Proteins directly control the nucleation and growth of biominerals, but the details of molecular recognition at the protein-biomineral interface remain poorly understood. The elucidation of recognition...
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[NMR paper] Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral
Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.
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J Magn Reson. 1999 Jan;136(1):86-91
Authors: Hong M
A technique for obtaining dipolar-mediated INADEQUATE NMR spectra with a large spectral window in the double-quantum dimension is presented. Using the dipolar recoupling sequence C7 to excite the double-quantum coherence under magic-angle spinning, the technique involves incrementing the...
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[NMR paper] Double and triple resonance NMR methods for protein assignment.
Double and triple resonance NMR methods for protein assignment.
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Methods Mol Biol. 1997;60:29-52
Authors: Whitehead B, Craven CJ, Waltho JP
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[NMR paper] Double and triple resonance NMR methods for protein assignment.
Double and triple resonance NMR methods for protein assignment.
Related Articles Double and triple resonance NMR methods for protein assignment.
Methods Mol Biol. 1997;60:29-52
Authors: Whitehead B, Craven CJ, Waltho JP
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[NMR paper] Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1990 Sep 4;29(35):8172-84
Authors: Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM
The assignment of the aliphatic 1H and 13C resonances of IL-1 beta, a protein of 153 residues and molecular...
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Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Jakob J. Lopez, Christoph Kaiser, Sarika Shastri and Clemens Glaubitz
Journal of Biomolecular NMR; 2008; 41(2) pp 97 - 104
Abstract:
13C homonuclear correlation spectra based on proton driven spin diffusion (PDSD) are becoming increasingly important for obtaining distance constraints from multiply labeled biomolecules by MAS NMR. One particular challenging situation arises when such constraints are to be obtained from spectra with a large natural abundance signal background which...