Measurement of HN-Hα J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
摘要：
Two new methods are described for the measurement of three-bond J H N H α couplings in proteins isotopically enriched with 15 N. 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 1 H- 15 N HMQC spectra, which are modulated in intensity by J H N H α , or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys 75 -Asp 80 have J H N H α values 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 Ca 2+ -ligated calmodulin.
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DOI：
10.1007/BF00398416
被引量：
年份：
1994
Springer
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