Abstract
Sensitivity-enhanced versions of the IPAP, TROSY–anti-TROSY, and E.COSY experiments for measuring one-bond 15 N– 1 H N couplings are presented. Together with the previously developed sensitivity-enhanced E.COSY-type HSQC experiment they comprise a suite of sensitivity-enhanced experiments that allows one to chose the optimal spectrum for accurate measurement of one-bond 15 N– 1 H N residual dipolar couplings in proteins. Since one-bond 15 N– 1 H N residual dipolar couplings play uniquely important roles in structural NMR, these additional methods provide further tools for improving structure determination of proteins and other biological macromolecules.
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