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Related Experiment Video

Updated: Jun 22, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Automated assignment in selectively methyl-labeled proteins.

Yingqi Xu1, Minhao Liu, Peter J Simpson

  • 1Division of Molecular Biosciences, Cross Faculty NMR Centre, Imperial College London, South Kensington, London, SW7 2AZ, UK.

Journal of the American Chemical Society
|June 19, 2009
PubMed
Summary

This study introduces an automated method for assigning methyl groups in large proteins using NMR spectroscopy. This technique significantly speeds up the process, assigning 99% of methyl groups without mutations.

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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

Published on: December 12, 2013

Area of Science:

  • Biochemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for determining protein structure and dynamics.
  • Transverse relaxation optimized spectroscopy (TROSY) and specific methyl labeling schemes have enabled NMR studies of larger proteins (up to 1 MDa).
  • Current methods for methyl group resonance assignment in large proteins rely on time-consuming mutagenesis or fragment analysis, which can complicate interpretation due to chemical shift perturbations.

Purpose of the Study:

  • To develop and validate a novel automated procedure for rapid methyl group resonance assignment in very large proteins.
  • To overcome the limitations of existing time-consuming and potentially confounding mutagenesis-based strategies.
  • To enable efficient structural and dynamic studies of large protein complexes via NMR.

Main Methods:

  • Development of an automated computational procedure for methyl group assignment.
  • Application of the method to an isoleucine, valine, and leucine (ILV)-labeled 300 kDa proteasome complex.
  • Utilizing high-quality NMR spectra recorded on the large protein system.

Main Results:

  • The automated procedure rapidly assigned the majority of methyl groups in the 300 kDa proteasome.
  • 99% of observed methyl groups were correctly assigned without manual intervention.
  • The method successfully bypasses the need for mutagenesis or fragment analysis.

Conclusions:

  • The developed automated procedure significantly accelerates methyl group assignment for very large proteins via NMR.
  • This approach offers a more efficient and reliable alternative to traditional methods, facilitating the study of large biomolecular systems.
  • The tool is publicly available (http://nmr.bc.ic.ac.uk/map-xs/) for broader scientific application.