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NMR processing:
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Ab initio:
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
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Homology-based:
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Torsion angles 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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RDCs:
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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:
MAXOCC
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:
camLILA
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Isotope labeling:
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Solid-state NMR:
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Default Determination of the electron relaxation rates in paramagnetic metal complexes: appli

Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.

Related Articles Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.

J Magn Reson. 2004 Apr;167(2):169-77

Authors: Jensen MR, Led JJ


Four different approaches for determining the electron relaxation rates in paramagnetic metallo-proteins are investigated, using a paramagnetic Ni2+ complex of a protein as an example. All four approaches rely on the determination of the longitudinal paramagnetic relaxation enhancements, R1p, of the 1H nuclei and the backbone 15N nuclei. Three of the methods utilize the field dependence of the R1p rates. It is found that the applicability of each of these methods depends on whether the fast-motion condition, omegaS2tau2
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