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Related Concept Videos

Proteomics01:33

Proteomics

7.2K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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Related Experiment Video

Updated: May 24, 2025

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

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Lossless single-molecule counting to absolute quantify proteoforms.

Tobias Gross1,2, Tobias Hundertmark1,2, Villő Csiszár3

  • 1Laboratory for MEMS Applications, Department of Microsystems Engineering, University of Freiburg, Georges-Köhler-Allee 103, Freiburg, 79110, Germany.

Scientific Reports
|March 2, 2025
PubMed
Summary
This summary is machine-generated.

A new assay, Protein Interaction Coupling (PICO), precisely quantifies proteoforms without external references. This digital, single-molecule method offers sensitive detection and multiplexing capabilities for cellular analysis.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Molecular Biology

Background:

  • Accurate quantification of proteoforms is crucial for understanding cellular processes.
  • Existing methods often require external references or lack sensitivity.
  • There is a need for precise, reference-free protein quantification techniques.

Purpose of the Study:

  • To introduce a novel immunoassay, Protein Interaction Coupling (PICO), for reference-free proteoform quantification.
  • To present the theoretical framework and validation of the PICO assay.
  • To demonstrate the capabilities of PICO in analytical and cellular matrices, including multiplexing.

Main Methods:

  • Development of a compartmentalized, homogeneous single-molecule assay (PICO).
  • Utilized a background-free, digital enumeration principle (decouplexing).
  • Validated PICO with recombinant and non-recombinant ErbB2 and peptide rTRX targets in various matrices.

Main Results:

  • PICO achieved precise, reference-free quantification of proteoforms, detecting down to a few molecules.
  • Demonstrated combinatorial multiplexing (cplex) with an 8-plex antibody assay.
  • Quantified functional changes in the ErbB pathway upon dactolisib treatment, revealing cellular stoichiometry.

Conclusions:

  • PICO provides a versatile, standardized, and accurate method for protein measurements.
  • The assay offers deep insights into physiological and perturbed cellular processes.
  • PICO has significant potential for advancing proteomic research and diagnostics.