AI Article Synopsis
- Novel E.COSY-type HSQC experiments enable precise measurement of one-bond 15N-1H and 15N-13C, as well as two-bond 13C-1H residual dipolar couplings in proteins.
- These experiments utilize fewer pulses than traditional methods, resulting in spectra that are 1.4 times more sensitive than standard coupled HSQC spectra.
- The improved measurement techniques are expected to significantly contribute to structural NMR studies for proteins and other biological macromolecules.
Article Abstract
Novel E.COSY-type HSQC experiments are presented for the accurate measurement of one-bond 15N-1H(N) and 15N-13C(') and two-bond 13C(')-1H(N) residual dipolar couplings in proteins. Compared with existing experiments, the (delta,J)-E.COSY experiments described here are composed of fewer pulses and the resulting spectra exhibit 1.4 times the sensitivity of coupled HSQC spectra. Since residual dipolar couplings play increasingly important roles in structural NMR, the proposed methods should find wide spread application for structure determination of proteins and other biological macromolecules.
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| http://dx.doi.org/10.1016/s1090-7807(02)00024-1 | DOI Listing |
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