AI Article Synopsis
- The study presents an advanced technique for measuring dipolar couplings in proteins using sensitivity-enhanced 2D IPAP experiments based on the accordion principle.
- The resulting spectra have resolution comparable to standard decoupled HSQC spectra, with 1D sensitivity slightly lower than traditional 3D pulse sequences.
- The pulse sequences can be adapted to 3D forms when needed, making them a useful tool for studying residual dipolar couplings in biological systems.
Article Abstract
Sensitivity-enhanced 2D IPAP experiments using the accordion principle for measuring one-bond 13C'-13Calpha and 1Halpha-13Calpha dipolar couplings in proteins are presented. The resolution of the resulting spectra is identical to that of the decoupled HSQC spectra and the sensitivity of the corresponding 1D acquisitions are only slightly lower than those obtained with 3D HNCO and 3D HN(COCA)HA pulse sequences due to an additional delay 2Delta. For cases of limited resolution in the 2D 15N-1HN HSQC spectrum the current pulse sequences can easily be modified into 3D versions by introducing a poorly digitized third dimension, if so desired. The experiments described here are a valuable addition to the suites available for determination of residual dipolar couplings in biological systems.
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| http://dx.doi.org/10.1016/j.jmr.2003.12.016 | DOI Listing |
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