We are analyzing https://link.springer.com/article/10.1007/bf00398416.

Title:
Measurement of HN-Hα J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods | Journal of Biomolecular NMR
Description:
Two new methods are described for the measurement of three-bond JH NHαcouplings in proteins isotopically enriched with 15N. Both methods leave the water magnetization in an unsaturated state, parallel to the z-axis, and therefore offer significant enhancements in sensitivity for rapidly exchanging backbone amide protons. The J couplings can be measured either from a set of constant-time 2D 1H-15N HMQC spectra, which are modulated in intensity by JH NHα, or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys75-Asp80 have JH NHαvalues in the 6–7 Hz range, suggesting that a break in the ‘central helix’ occurs at the same position as previously observed in solution NMR studies of Ca2+-ligated calmodulin.
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3d water-flip-back methods water-flip-back version month download article/chapter privacy choices/manage cookies 3d hnha experiment calcium-free calmodulin ca2+-ligated calmodulin biomolecular nmr aims full article pdf solution nmr studies european economic area proteins isotopically enriched offer significant enhancements residues lys75-asp80 �central helix’ occurs conditions privacy policy accepting optional cookies 1007/bf00398416 keywords journal finder publish main content log bond jh nhαcouplings check access instant access water magnetization hitoshi kuboniwa methods leave unsaturated state related subjects article kuboniwa privacy policy article journal personal data books a optional cookies manage preferences article log journal publish subscription content delaglio data protection essential cookies cookies skip biomol nmr 4 institution subscribe methods article cite jh nhα jh nhαvalues usage analysis social media

Schema {🗺️}

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         description:Two new methods are described for the measurement of three-bond JH NHαcouplings in proteins isotopically enriched with 15N. Both methods leave the water magnetization in an unsaturated state, parallel to the z-axis, and therefore offer significant enhancements in sensitivity for rapidly exchanging backbone amide protons. The J couplings can be measured either from a set of constant-time 2D 1H-15N HMQC spectra, which are modulated in intensity by JH NHα, or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys75-Asp80 have JH NHαvalues in the 6–7 Hz range, suggesting that a break in the ‘central helix’ occurs at the same position as previously observed in solution NMR studies of Ca2+-ligated calmodulin.
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      headline:Measurement of HN-Hα J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
      description:Two new methods are described for the measurement of three-bond JH NHαcouplings in proteins isotopically enriched with 15N. Both methods leave the water magnetization in an unsaturated state, parallel to the z-axis, and therefore offer significant enhancements in sensitivity for rapidly exchanging backbone amide protons. The J couplings can be measured either from a set of constant-time 2D 1H-15N HMQC spectra, which are modulated in intensity by JH NHα, or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys75-Asp80 have JH NHαvalues in the 6–7 Hz range, suggesting that a break in the ‘central helix’ occurs at the same position as previously observed in solution NMR studies of Ca2+-ligated calmodulin.
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      dateModified:
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