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Specific 15N, NH correlations for residues in15 N, 13C and fractionally deuterated proteins that immediately follow methyl-containing amino acids

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Abstract

A triple-resonance pulse scheme is described which records15N, NH correlations of residues that immediately follow amethyl-containing amino acid. The experiment makes use of a15N, 13C and fractionally deuterated proteinsample and selects for CH2D methyl types. The experiment isthus useful in the early stages of the sequential assignment process as wellas for the confirmation of backbone 15N, NH chemical shiftassignments at later stages of data analysis. A simple modification of thesequence also allows the measurement of methyl side-chain dynamics. This isparticularly useful for studying side-chain dynamic properties in partiallyunfolded and unfolded proteins where the resolution of aliphatic carbon andproton chemical shifts is limited compared to that of amide nitrogens.

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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, ON, Canada, M5S 1A8

    D.R. Muhandiram, Daiwen Yang, Ouwen Zhang & Lewis E. Kay

  2. The Protein Engineering Centers of Excellence, Department of Chemistry and Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada, V6T 1Z3

    Philip E. Johnson & Lawrence P. McIntosh

Authors
  1. D.R. Muhandiram
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  2. Philip E. Johnson
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  3. Daiwen Yang
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  4. Ouwen Zhang
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  5. Lawrence P. McIntosh
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  6. Lewis E. Kay
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Muhandiram, D., Johnson, P.E., Yang, D. et al. Specific 15N, NH correlations for residues in15 N, 13C and fractionally deuterated proteins that immediately follow methyl-containing amino acids. J Biomol NMR 10, 283–288 (1997). https://doi.org/10.1023/A:1018301818803

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