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Related Experiment Video

Updated: Nov 9, 2025

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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Label-Free Method Development for Hydroxyproline PTM Mapping in Human Plasma Proteome.

Debabrata Dutta1,2, Shakilur Rahman1, Gourab Bhattacharje1

  • 1Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur, 721302, India.

The Protein Journal
|April 11, 2021
PubMed
Summary
This summary is machine-generated.

This study introduces a new method to identify hydroxylated proteins in human plasma. The research identified 11 hydroxylated plasma proteins, including a key modification in Immunoglobulin A1 (IgA1), advancing proteomic analysis.

Keywords:
HydroxyprolineImmunoglobulinLabel-free methodsMS/MSMolecular dynamics simulationPlasma proteomicsPost-translational modifications

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Area of Science:

  • Biochemistry
  • Proteomics
  • Mass Spectrometry

Background:

  • Post-translational modifications (PTMs) create protein diversity, affecting function in disease.
  • Identifying PTMs in complex samples like plasma using untargeted proteomics remains challenging.

Purpose of the Study:

  • To develop and apply a label-free method for identifying and mapping hydroxylated proteins in human plasma.
  • To characterize the structural impact of proline hydroxylation in plasma proteins.

Main Methods:

  • Untargeted proteomics using tandem mass spectrometry (MS/MS).
  • Label-free quantification and de novo sequencing of peptides.
  • Molecular dynamics (MD) simulations to analyze structural changes.

Main Results:

  • Identified 676 de novo sequenced peptides from 201 human plasma proteins.
  • Discovered 11 hydroxylated plasma proteins, including Immunoglobulin A1 (IgA1) heavy chain.
  • Confirmed proline hydroxylation at residue 285 (Pro285 to Hyp285) in IgA1, causing significant structural alterations.

Conclusions:

  • The study presents a robust method for identifying hydroxyproline (Hyp) post-translational modifications in plasma.
  • The findings provide insights into the hydroxylated proteome of human plasma.
  • This approach can differentiate hydroxylated PTMs in normal versus diseased states.