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   <subfield code="a">A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins</subfield>
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   <subfield code="c">[Stephan Grzesiek, Ad Bax]</subfield>
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   <subfield code="a">Recently, a quantitative J correlation technique has been presented that permits measurementof 3JC′C′ in proteins isotopically enriched with 13C [Hu, J.-S. and Bax, A.(1996) J. Am. Chem. Soc., 118, 8170-8171]. Here, we describe an analogousexperiment that is less sensitive to transverse 13C′ relaxation, which is the principallimiting factor in all 13C-13C long-range correlation experiments on macromolecules. Thenew scheme utilizes homonuclear Hartmann-Hahn cross polarization (TOCSY) insteadof a COSY-type transfer to accomplish magnetization transfer; a description of the relevantrelaxation terms is presented. The experiment is demonstrated for ubiquitin and HIV-1 Nef.The results show excellent agreement between 3JC′C′ values measured forubiquitin with the new scheme and those reported previously. The experiment is particularlyuseful for distinguishing backbone φ angles that are smaller than -120° from thoselarger than -120°.</subfield>
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