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An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins

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Abstract

A triple resonance pulse scheme is presented for recording 13Cα-1Hα one-bond dipolar couplings in 15N, 13C labeled proteins. HNCO correlation maps are generated where the carbonyl chemical shift is modulated by the 13Cα-1Hα coupling, with the two doublet components separated into individual data sets. The experiment makes use of recently described methodology whereby the protein of interest is dissolved in a dilute solution of bicelles which orient above a critical temperature, thus permitting measurement of significant couplings (Tjandra and Bax, 1997a). An application to the protein ubiquitin is described.

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Authors and Affiliations

  1. The Protein Engineering Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, ON, Canada, M5S 1A8

    Daiwen Yang, Joel R. Tolman & Lewis E. Kay

  2. Department of Biochemistry, University of Toronto, Toronto, ON, Canada, M5S 1A8

    Natalie K. Goto

Authors
  1. Daiwen Yang
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  2. Joel R. Tolman
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  3. Natalie K. Goto
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  4. Lewis E. Kay
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Yang, D., Tolman, J.R., Goto, N.K. et al. An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins. J Biomol NMR 12, 325–332 (1998). https://doi.org/10.1023/A:1008223017233

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