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Heteronuclear 2D-correlations in a uniformly [13C, 15N] labeled membrane-protein complex at ultra-high magnetic fields

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Abstract

One- and two-dimensional solid-state NMR experiments on a uniformly labeled intrinsic membrane-protein complex at ultra-high magnetic fields are presented. Two-dimensional backbone and side-chain correlations for a [U-13C,15N] labeled version of the LH2 light-harvesting complex indicate significant resolution at low temperatures and under Magic Angle Spinning. Tentative assignments of some of the observed correlations are presented and attributed to the α-helical segments of the protein, mostly found in the membrane interior.

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Authors and Affiliations

  1. Gorlaeus Laboratories, The Netherlands

    T.A. Egorova-Zachernyuk, J. Hollander, H.J.M. de Groot & M. Baldus

  2. Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow, G12 8QQ, U.K

    N. Fraser & R. Cogdell

  3. Huygens Laboratories, Leiden University, 2333 CC, Leiden, The Netherlands

    P. Gast & A.J. Hoff

Authors
  1. T.A. Egorova-Zachernyuk
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  2. J. Hollander
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  3. N. Fraser
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  4. P. Gast
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  5. A.J. Hoff
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  6. R. Cogdell
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  7. H.J.M. de Groot
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  8. M. Baldus
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Egorova-Zachernyuk, T., Hollander, J., Fraser, N. et al. Heteronuclear 2D-correlations in a uniformly [13C, 15N] labeled membrane-protein complex at ultra-high magnetic fields. J Biomol NMR 19, 243–253 (2001). https://doi.org/10.1023/A:1011235417465

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