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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

10.1016/0009-2509(59)85004-1

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1573-5001

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Statistical removal of background signals from hig

Authors: Bradley Worley Nicholas J Sisco Robert Powers
Publish Date: 2015/07/09
Volume: 63, Issue: 1, Pages: 53-58
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Abstract

NMR ligandaffinity screens are vital to drug discovery are routinely used to screen fragmentbased libraries and used to verify chemical leads from highthroughput assays and virtual screens NMR ligandaffinity screens are also a highly informative first step towards identifying functional epitopes of unknown proteins as well as elucidating the biochemical functions of protein–ligand interaction at their binding interfaces While simple onedimensional 1H NMR experiments are capable of indicating binding through a change in ligand line shape they are plagued by broad illdefined background signals from protein 1H resonances We present an uncomplicated method for subtraction of protein background in highthroughput ligandbased affinity screens and show that its performance is maximized when phasescatter correction is applied prior to subtraction

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  2. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK
  3. 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
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  5. Insights into furanose solution conformations: beyond the two-state model
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  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
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  22. Erratum to: 13 C α CEST experiment on uniformly 13 C-labeled proteins
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