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Ab initio:
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Refinement:
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Structure from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Isotope labeling:
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Solid-state NMR:
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Default 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.

Related Articles Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.

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 evolution period in synchrony with the phase of the radiofrequency pulses in the C7 sequence. The technique is demonstrated on a uniformly 13C-labeled amino acid and an extensively 13C-labeled protein to identify 13C connectivity patterns for spectral assignment.

PMID: 9887293 [PubMed - indexed for MEDLINE]



Source: PubMed
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