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Estimates of methyl 13C and 1H CSA values (Δσ) in proteins from cross-correlated spin relaxation

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Abstract

Simple pulse schemes are presented for the measurement of methyl 13C and 1H CSA values from 1H–13C dipole/13C CSA and 1H–13C dipole/1H CSA cross-correlated relaxation. The methodology is applied to protein L and malate synthase G. Average 13C CSA values are considerably smaller for Ile than Leu/Val (17 vs 25 ppm) and are in good agreement with previous solid state NMR studies of powders of amino acids and dipeptides and in reasonable agreement with quantum-chemical DFT calculations of methyl carbon CSA values in peptide fragments. Small averaged 1H CSA values on the order of 1 ppm are measured, consistent with a solid state NMR determination of the methyl group 1H CSA in dimethylmalonic acid.

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Authors and Affiliations

  1. Protein Engineering Network Center of Excellence, Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ont, Canada, M5S 1A8

    Vitali Tugarinov & Lewis E. Kay

  2. Lehrstuhl für Theoretische Chemie, Technische Universität München, 85748, Garching, Germany

    Christoph Scheurer

  3. Gustaf H. Carlson School of Chemistry, Clark University, Worcester, Massachusetts, 01610, U.S.A

    Rafael Brüschweiler

Authors
  1. Vitali Tugarinov
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  2. Christoph Scheurer
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  3. Rafael Brüschweiler
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  4. Lewis E. Kay
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Tugarinov, V., Scheurer, C., Brüschweiler, R. et al. Estimates of methyl 13C and 1H CSA values (Δσ) in proteins from cross-correlated spin relaxation. J Biomol NMR 30, 397–406 (2004). https://doi.org/10.1007/s10858-004-4349-x

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  • DOI: https://doi.org/10.1007/s10858-004-4349-x

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