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Sequence-specific assignment of histidine and tryptophan ring 1H, 13C and 15N resonances in 13C/15N- and 2H/13C/15N-labelled proteins

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Abstract

Methods are described to correlate aromatic 1Hδ 2/13Cδ 2 or 1Hε 1/15Nε 1 with aliphatic 13Cβ chemical shifts of histidine and tryptophan residues, respectively. The pulse sequences exclusively rely on magnetization transfers via one-bond scalar couplings and employ [15N, 1H]- and/or [13C, 1H]-TROSY schemes to enhance sensitivity. In the case of histidine imidazole rings exhibiting slow HN-exchange with the solvent, connectivities of these proton resonances with β-carbons can be established as well. In addition, their correlations to ring carbons can be detected in a simple [15N, 1H]-TROSY-H(N)Car experiment, revealing the tautomeric state of the neutral ring system. The novel methods are demonstrated with the 23-kDa protein xylanase and the 35-kDa protein diisopropylfluorophosphatase, providing nearly complete sequence-specific resonance assignments of their histidine δ-CH and tryptophan ε-NH groups.

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Authors and Affiliations

  1. Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt am Main, Biozentrum N230, 1. OG, Marie Curie-Strasse 9, D-60439, Frankfurt, Germany

    Frank Löhr, Vicky Katsemi, Marco Betz, Judith Hartleib & Heinz Rüterjans

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  1. Frank Löhr
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  2. Vicky Katsemi
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  3. Marco Betz
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  4. Judith Hartleib
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  5. Heinz Rüterjans
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Correspondence to Frank Löhr.

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Löhr, F., Katsemi, V., Betz, M. et al. Sequence-specific assignment of histidine and tryptophan ring 1H, 13C and 15N resonances in 13C/15N- and 2H/13C/15N-labelled proteins. J Biomol NMR 22, 153–164 (2002). https://doi.org/10.1023/A:1014271204953

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