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Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins

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Summary

Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC is a novel experiment for aromatic spin system identification in uniformly 13C-labeled proteins, which is implemented so that it correlates the chemical shift of a given aromatic proton with those of the directly attached carbon and all vicinal protons. The ct-HMQC scheme is used both for overlay of the indirect 1H and 13C chemical shift evolution periods and for the generation of 1H-1H antiphase magnetization to accelerate the 1H-TOCSY magnetization transfer at short mixing times. As an illustration, data recorded for the 18 kDa protein cyclophilin A are presented. Since transverse relaxation of 13C-1H zero-quantum and double-quantum coherences is to first order insensitive to 13C-1H heteronuclear dipolar relaxation, the new experiment should work also for proteins with molecular weights above 20 kDa.

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Authors and Affiliations

  1. Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, CH-8093, Zürich, Switzerland

    Oliver Zerbe, Thomas Szyperski, Marcel Ottiger & Kurt Wüthrich

  2. Departement für Pharmazie, ETH, CH-8057, Zürich, Switzerland

    Oliver Zerbe

Authors
  1. Oliver Zerbe
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  2. Thomas Szyperski
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  3. Marcel Ottiger
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  4. Kurt Wüthrich
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Zerbe, O., Szyperski, T., Ottiger, M. et al. Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins. J Biomol NMR 7, 99–106 (1996). https://doi.org/10.1007/BF00203820

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  • DOI: https://doi.org/10.1007/BF00203820

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