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Detergent Purification of Membrane Proteins

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Related Experiment Video

Updated: Jun 16, 2026

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

Membrane protein solubilization.

Katia Duquesne¹, James N Sturgis

¹Institut de Biologie Structurale et Microbiologie, CNRS and Aix Marseille Université, France.

Methods in Molecular Biology (Clifton, N.J.)

|January 26, 2010

Summary

Solubilizing membrane proteins for in vitro analysis requires carefully disrupting lipids while maintaining protein integrity in detergents. This chapter outlines general principles for successful membrane protein extraction and stabilization.

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

In vitro analysis of membrane proteins necessitates their extraction from the lipid bilayer.
Solubilization aims to disrupt lipids while preserving protein structure and function in a detergent environment.

Purpose of the Study:

To establish general principles for the successful solubilization of membrane proteins.
To present a method for obtaining active membrane protein complexes in aqueous solution.

Main Methods:

Careful disruption of membrane lipid components.
Complexation of membrane proteins with detergents to form an aqueous solution.
Maintaining protein integrity within an unnatural detergent environment.

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Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Published on: August 14, 2011

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Last Updated: Jun 16, 2026

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

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Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Published on: August 14, 2011

Main Results:

Successful solubilization of an increasing number of membrane proteins in active forms.
Establishment of general principles governing the solubilization process.
Development of a specific method for membrane protein extraction.

Conclusions:

Membrane protein solubilization is a delicate but achievable process.
Understanding general principles is key to mastering membrane protein extraction.
The presented method facilitates purification and further analysis of membrane proteins.