Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins |
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Authors: | Oliver Zerbe Thomas Szyperski Marcel Ottiger Kurt Wüthrich |
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Institution: | (1) Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, CH-8093 Zürich, Switzerland;(2) Departement für Pharmazie, ETH, CH-8057 Zürich, Switzerland |
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Abstract: | 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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Keywords: | Resonance assignments Aromatic spin systems 13C-labeled proteins HMQC |
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