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Related Experiment Videos

Molecular clocks.

N E Robinson1, A B Robinson

  • 1Department of Chemistry, California Institute of Technology, Pasadena, CA 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America
|February 7, 2001
PubMed
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A new mass spectrometry method precisely measures deamidation rates in peptides and proteins. This technique quantifies how protein structure impacts deamidation, potentially serving as biological event timers.

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Deamidation of glutaminyl and asparaginyl residues is a common post-translational modification.
  • Understanding deamidation rates is crucial for protein stability and function studies.
  • Existing methods for measuring deamidation rates can be imprecise or cumbersome.

Purpose of the Study:

  • To develop a precise and convenient mass spectrometric method for quantifying deamidation rates.
  • To determine deamidation rates for numerous asparaginyl sequences in model peptides.
  • To investigate the influence of protein structure on deamidation kinetics.

Main Methods:

  • Development of a mass spectrometry-based assay for deamidation rate measurement.
  • Determination of deamidation rates for 306 asparaginyl sequences in model peptides under defined conditions (pH 7.4, 37°C, 0.15 M Tris.HCl).

Related Experiment Videos

  • Simultaneous deamidation rate measurements of rabbit muscle aldolase and model peptides to assess structural effects.

    • Main Results:

    • A library of 913 amide-containing peptides was established for deamidation studies.
    • Deamidation rates for 306 asparaginyl sequences were determined.
    • The method successfully demonstrated the impact of primary, secondary, tertiary, and quaternary protein structures on deamidation rates.

    Conclusions:

    • The developed mass spectrometry method is a valuable tool for precise deamidation rate measurements.
    • Protein structure significantly influences the rate of glutaminyl and asparaginyl residue deamidation.
    • Deamidation of these residues may function as molecular timers for biological events.