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Updated: Mar 25, 2026

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Neucode Labels for Multiplexed, Absolute Protein Quantification.

Gregory K Potts^1,2, Emily A Voigt^3,4, Derek J Bailey^1,2

¹Department of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.

Analytical Chemistry

|February 17, 2016

Summary

This summary is machine-generated.

We present a new method for multiplexed, absolute protein quantification using neutron encoding (NeuCode) and parallel reaction monitoring (PRM). This technique allows for up to 30 channels of quantitative data in a single mass spectrometry experiment, ideal for studying viral infections.

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Area of Science:

Proteomics
Mass Spectrometry
Molecular Biology

Background:

Accurate protein quantification is crucial for understanding cellular processes and disease.
Existing methods for multiplexed protein quantification often face limitations in dynamic range and throughput.
Targeted mass spectrometry approaches offer high specificity but can be challenging to multiplex effectively.

Purpose of the Study:

To develop a novel method for multiplexed, absolute protein quantification.
To leverage the neutron encoding (NeuCode) metabolic labeling strategy with parallel reaction monitoring (PRM).
To demonstrate the application of this combined approach for monitoring viral infection dynamics.

Main Methods:

Utilized the neutron encoding (NeuCode) metabolic labeling strategy for peptide labeling.
Employed parallel reaction monitoring (PRM) on high-resolution tandem mass spectrometry.
Applied the NeuCode-PRM method to cultured cells to monitor viral infection time points.

Main Results:

Successfully achieved multiplexed, absolute protein quantification.
Demonstrated the ability to monitor viral protein production over multiple infection time points in a single experiment.
The NeuCode-PRM combination enabled up to 30 channels of quantitative information per MS experiment.

Conclusions:

The NeuCode-PRM method provides a powerful platform for high-throughput, targeted protein quantification.
This approach significantly enhances multiplexing capabilities in mass spectrometry-based proteomics.
The method is well-suited for dynamic studies, such as monitoring viral infections and protein expression changes over time.