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Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

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Related Experiment Video

Updated: Dec 11, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

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Published on: August 6, 2018

Multiplexed Proximity Biotinylation Coupled to Mass Spectrometry for Defining Integrin Adhesion Complexes.

Megan R Chastney¹, Craig Lawless¹, Martin J Humphries¹

¹Faculty of Biology, Medicine & Health, Wellcome Centre for Cell-Matrix Research, Manchester Academic Health Science Centre, University of Manchester, Michael Smith Building, Oxford Road, Manchester, United Kingdom.

Current Protocols in Cell Biology

|August 25, 2020

Summary

Proximity biotinylation using BioID effectively maps protein interactions in integrin adhesion complexes (IACs). This method identifies novel interactors and reveals complex architecture, aiding in understanding cellular structures.

Keywords:

BioID cell-extracellular matrix adhesion integrin adhesion complexes mass spectrometry proximity-dependent labeling

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Last Updated: Dec 11, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

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Published on: August 6, 2018

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

Published on: May 17, 2020

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

Area of Science:

Cell Biology
Biochemistry

Background:

Traditional methods struggle with insoluble and transient proteins in complexes.
Integrin adhesion complexes (IACs) link the plasma membrane to the actin cytoskeleton.
Understanding IAC architecture is crucial for cellular processes.

Purpose of the Study:

To apply BioID proximity biotinylation to study IACs.
To identify novel proximal interactors of IACs.
To gain insights into IAC architecture and protein network topology.

Main Methods:

Utilized BioID proximity-dependent biotinylation.
Employed multiple BioID baits for complex-wide annotation.
Performed label-free quantitative mass spectrometry for protein analysis.
Conducted bioinformatic analyses for network interrogation.

Main Results:

Successfully mapped IAC-proximal proteins.
Identified novel interactors and provided spatial annotation.
Enabled insights into IAC architecture and protein network topology.
Established protocols for BioID application in IAC studies.

Conclusions:

BioID is a powerful technique for studying protein complexes like IACs.
This approach facilitates the discovery of novel interactors and understanding of complex organization.
The described methods provide a framework for future proximity interactome studies.