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Title of Journal: J Biomol NMR

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Abbravation: Journal of Biomolecular NMR

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Springer Netherlands

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DOI

10.1007/3-540-48743-3

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1573-5001

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NOESYWaterControl a new NOESY sequence for the o

Authors: Allan M Torres Gang Zheng William S Price
Publish Date: 2017/03/07
Volume: 67, Issue: 3, Pages: 233-241
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Abstract

Highly selective and efficient water signal suppression is indispensable in biomolecular 2D nuclear Overhauser effect spectroscopy NOESY experiments However the application of conventional water suppression schemes can cause a significant or complete loss of the biomolecular resonances at and around the water chemical shift ω2 In this study a new sequence NOESYWaterControl was developed to address this issue The new sequence was tested on lysozyme and bovine pancreatic trypsin inhibitor BPTI demonstrating its efficiency in both water suppression and more excitingly preserving waterproximate biomolecular resonances in ω2 The 2D NOESY maps obtained using the new sequence thus provide more information than the maps obtained with conventional water suppression thereby lessening the number of experiments needed to complete resonance assignments of biomolecules The 2D NOESYWaterControl map of BPTI showed strong bound water and exchangeable proton signals in ω1 but these signals were absent in ω2 indicating the possibility of using the new sequence to discriminate bound water and exchangeable proton resonances from nonlabile proton resonances with similar chemical shifts to water

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Other Papers In This Journal:
  1. Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent
  2. Statistical removal of background signals from high-throughput 1 H NMR line-broadening ligand-affinity screens
  3. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK
  4. HNHC: a triple resonance experiment for correlating the H2, N1(N3) and C2 resonances in adenine nucleobases of 13 C-, 15 N-labeled RNA oligonucleotides
  5. Insights into furanose solution conformations: beyond the two-state model
  6. Selective 1 H- 13 C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
  7. Fast methionine-based solution structure determination of calcium-calmodulin complexes
  8. A procedure to validate and correct the 13 C chemical shift calibration of RNA datasets
  9. Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding
  10. NMR solution structure of the acylphosphatase from Escherichia coli
  11. A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
  12. S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments
  13. Improved NMR experiments with 13 C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins
  14. Out-and-back 13 C– 13 C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS
  15. Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization
  16. A probe to monitor performance of 15 N longitudinal relaxation experiments for proteins in solution
  17. Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
  18. Use of quantitative 1 H NMR chemical shift changes for ligand docking into barnase
  19. Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy
  20. Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy
  21. Hexagonal ice in pure water and biological NMR samples
  22. Erratum to: 13 C α CEST experiment on uniformly 13 C-labeled proteins
  23. Auto-inducing media for uniform isotope labeling of proteins with 15 N, 13 C and 2 H
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