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Deamidation of human proteins.

N E Robinson1, A B Robinson

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. noahr@its.caltech.edu

Proceedings of the National Academy of Sciences of the United States of America
|October 19, 2001
PubMed
Summary

Asparagine and glutamine deamidation alters protein charge and shape over time. Calculations show this deamidation is a significant biological process affecting many human proteins.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Deamidation of asparaginyl and glutaminyl residues is a post-translational modification.
  • This modification can alter protein structure, function, and stability.
  • Understanding deamidation rates is crucial for interpreting protein behavior in biological systems.

Purpose of the Study:

  • To quantitatively predict the deamidation rates of asparaginyl residues in human proteins.
  • To assess the biological relevance of deamidation across a large set of human proteins.

Main Methods:

  • Performed quantitative and experimentally verified predictive calculations.
  • Analyzed 1,371 asparaginyl residues within 126 diverse human proteins.

Main Results:

  • Calculated deamidation rates for a substantial number of asparaginyl residues.
  • Identified that deamidation significantly impacts protein charge and conformation.
  • Found deamidation to be a relevant phenomenon in a large percentage of human proteins studied.

Conclusions:

  • Deamidation of asparagine and glutamine residues is a widespread and biologically significant process.
  • The calculated rates provide valuable data for predicting protein stability and function.
  • This study highlights the importance of considering deamidation in proteomics and drug development.

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