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A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle ψ Based on Cross-correlation Between 13Cα-1Hα Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions

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Abstract

A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.

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Authors and Affiliations

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

    Daiwen Yang, Kevin H. Gardner & Lewis E. Kay

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  1. Daiwen Yang
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  2. Kevin H. Gardner
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  3. Lewis E. Kay
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Yang, D., Gardner, K.H. & Kay, L.E. A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle ψ Based on Cross-correlation Between 13Cα-1Hα Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions. J Biomol NMR 11, 213–220 (1998). https://doi.org/10.1023/A:1008284315816

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