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Radiation damping in modern NMR experiments: progress and challenges.

Radiation damping in modern NMR experiments: progress and challenges.

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Biomolecular ligands screening using radiation damping difference WaterLOGSY spectroscopy.Measuring hydrogen exchange in proteins by selective water saturation in (1)H- (15)N SOFAST/BEST-type experiments: advantages and limitations.Sensitive imaging of magnetic nanoparticles for cancer detection by active feedback MR.An optimized method for (15)N R(1) relaxation rate measurements in non-deuterated proteins.Gradient-based solvent suppression methods on a benchtop spectrometer.Effects of radiation damping for biomolecular NMR experiments in solution: a hemisphere concept for water suppression High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids Protein-Inhibitor Interaction Studies Using NMR Acquiring and processing ultrafast biomolecular 2D NMR experiments using a referenced-based correction.Ultrafast multidimensional Laplace NMR for a rapid and sensitive chemical analysis In vivo characterization of the downfield part of (1) H MR spectra of human brain at 9.4 T: Magnetization exchange with water and relation to conventionally determined metabolite content.The new face of isotopic NMR at natural abundance.

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Radiation damping in modern NMR experiments: progress and challenges.

http://www.wikidata.org/entity/Q40399095

description

2012 nî lūn-bûn

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Radiation damping in modern NMR experiments: progress and challenges.

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Radiation damping in modern NMR experiments: progress and challenges.

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Radiation damping in modern NMR experiments: progress and challenges.

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J.PNMRS.2012.06.001

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Progress in Nuclear Magnetic Resonance Spectroscopy

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Radiation damping in modern NMR experiments: progress and challenges.

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Nagarajan Murali

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V V Krishnan

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P2860

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Structural basis for the selectivity of the external thioesterase of the surfactin synthetase

Protein structure determination in living cells by in-cell NMR spectroscopy

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin.

Optimal isotope labelling for NMR protein structure determinations.

Use of a water flip-back pulse in the homonuclear NOESY experiment.

Selective excitation of intense solvent signals in the presence of radiation damping.

Perfusion imaging using FAIR with a short predelay.

Radiation damping compensation of selective pulses in water-protein exchange spectroscopy.

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41-57

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scholarly article

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10.1016/J.PNMRS.2012.06.001

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68

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2012-06-15T00:00:00Z

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