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Updated: Jul 26, 2026
08:01
LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Deamidation of human proteins.
1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. noahr@its.caltech.edu
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.
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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