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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

10.1016/0191-491x(83)90013-5

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ISSN

1573-5001

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Use of quantitative Superscript1/SuperscriptH

Authors: Marina Cioffi Christopher A Hunter Martin J Packer Maya J Pandya Mike P Williamson
Publish Date: 2008/11/01
Volume: 43, Issue: 1, Pages: 11-
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Abstract

1H NMR complexationinduced changes in chemical shift CIS of HN protons have been used to characterize the complexes of barnase with the deoxyoligonucleotides dGC and dCGAC Quantitative shift changes are used not only to locate the most probable binding site using ringcurrent shifts but also to determine the orientation of the ligand within the binding site based on a more complete shift calculation including bond magnetic anisotropies and electric field effects For both ligands the guanine is in the same binding site cleft in the same position as identified in the crystal structure of the dCGAC complex By contrast a previous Xray crystal structure of the dGC complex showed the ligand in the mouth of the active site rather than at the guanylspecific site implying that the location may be an artifact of the crystallisation process


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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. NOESY-WaterControl: a new NOESY sequence for the observation of under-water protein resonances
  6. Insights into furanose solution conformations: beyond the two-state model
  7. Selective 1 H- 13 C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
  8. Fast methionine-based solution structure determination of calcium-calmodulin complexes
  9. A procedure to validate and correct the 13 C chemical shift calibration of RNA datasets
  10. Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding
  11. NMR solution structure of the acylphosphatase from Escherichia coli
  12. A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
  13. S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments
  14. Improved NMR experiments with 13 C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins
  15. Out-and-back 13 C– 13 C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS
  16. Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization
  17. A probe to monitor performance of 15 N longitudinal relaxation experiments for proteins in solution
  18. Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
  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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