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Measurement of the protein backbone dihedral angle φ based on quantification of remote CSA/DD interference in inter-residue 13C′(i − 1)-13Cα(i) multiple-quantum coherences

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Abstract

A novel triple-resonance NMR method is presented for the measurement of the protein backbone dihedral angle φ based on differential multiple-quantum relaxation induced by relaxation interference between 1Hα(i)-13Cα(i) dipolar and 13C′(i−1) (carbonyl) chemical shift anisotropy mechanisms. The method employs a simultaneous transfer of 15N magnetization to the inter- and intra-residue 13Cα carbons as well as the directly attached carbonyl carbon 13C′. Results obtained on 13C,15N-labeled ubiquitin demonstrate the potential of the method.

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Authors and Affiliations

  1. Institute of Organic Chemistry, University of Innsbruck, Innrain 52a, A-6020, Innsbruck, Austria

    Karin Kloiber & Robert Konrat

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  1. Karin Kloiber
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  2. Robert Konrat
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Kloiber, K., Konrat, R. Measurement of the protein backbone dihedral angle φ based on quantification of remote CSA/DD interference in inter-residue 13C′(i − 1)-13Cα(i) multiple-quantum coherences. J Biomol NMR 17, 265–268 (2000). https://doi.org/10.1023/A:1008393903160

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