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Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Complex Assembly

Protein Complex Assembly

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Affinity and Avidity

Affinity and Avidity

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Related Experiment Video

Updated: Feb 8, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP).

Jordan F Hastings¹, Jeremy Z R Han¹, Robert F Shearer²

¹The Kinghorn Cancer Centre, Garvan Institute of Medical Research.

Journal of Visualized Experiments : Jove

|July 10, 2018

Summary

This summary is machine-generated.

Researchers developed Bimolecular Complementation Affinity Purification (BiCAP) to specifically isolate and study protein complexes. This new method enhances understanding of cell signaling pathways and protein interactions in disease.

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Last Updated: Feb 8, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

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Bimolecular Fluorescence Complementation

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Published on: April 15, 2011

Area of Science:

Biochemistry
Cell Biology
Proteomics

Background:

Protein complex assembly regulates cell signaling pathways.
Dysregulation of protein complexes is implicated in various diseases.
Existing techniques lack specificity and sensitivity for analyzing multi-molecular signaling complexes.

Purpose of the Study:

To address the limitations of current experimental techniques for analyzing protein complexes.
To develop a novel method for specific and sensitive deconvolution of multi-molecular signaling complexes.

Main Methods:

Developed Bimolecular Complementation Affinity Purification (BiCAP).
BiCAP combines a protein complementation assay with a conformation-specific nanobody.
This technique enables specific isolation and proteomic characterization of interacting protein pairs.

Main Results:

BiCAP specifically isolates target protein pairs, excluding un-complexed proteins and non-specific binders.
The technique demonstrates high specificity, surpassing standard affinity purification methods.
BiCAP is adaptable to various downstream experimental assays.

Conclusions:

BiCAP offers a novel and highly specific approach for studying protein complex assembly.
This technique facilitates more nuanced investigations into the mechanics of cell signaling.
BiCAP advances the study of protein interactions in both normal biological processes and disease states.