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Related Concept Videos

Detergent Purification of Membrane Proteins01:18

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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Related Experiment Video

Updated: May 28, 2026

High-throughput Crystallization of Membrane Proteins Using the Lipidic Bicelle Method
07:26

High-throughput Crystallization of Membrane Proteins Using the Lipidic Bicelle Method

Published on: January 9, 2012

Crystallizing membrane proteins using lipidic bicelles.

Rachna Ujwal1, James U Bowie

  • 1Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, Molecular Biology Institute, UCLA, Los Angeles, CA 90095-1570, United States.

Methods (San Diego, Calif.)
|October 11, 2011
PubMed
Summary
This summary is machine-generated.

Bicelles, discoidal lipid-protein complexes, offer a powerful method for crystallizing membrane proteins that resist traditional techniques. This lipidic phase crystallization approach maintains protein function and facilitates structural studies.

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09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

Area of Science:

  • Structural Biology
  • Biophysics
  • Membrane Protein Research

Background:

  • Crystallizing membrane proteins is difficult, especially for those resistant to detergent-based methods.
  • Lipidic phase crystallization offers an alternative for challenging protein targets.

Purpose of the Study:

  • To highlight the utility of bicelles for membrane protein crystallization.
  • To present bicelles as a viable alternative to traditional detergent-based methods.

Main Methods:

  • Utilizing bicelles, which are bilayer discs formed from phospholipids and amphiphiles.
  • Reconstituting membrane proteins into bicelles to mimic native environments.
  • Employing standard crystallization equipment for protein-bicelle mixtures.

Main Results:

  • Bicelles provide a native-like lipidic environment for membrane proteins.
  • Proteins reconstituted in bicelles remain functional under physiological conditions.
  • Successful crystallization of various membrane proteins, including bacteriorhodopsin and β2 adrenergic receptor, using bicelles.

Conclusions:

  • Bicelles are an effective medium for membrane protein crystallization.
  • The bicelle method is compatible with high-throughput screening and standard laboratory equipment.
  • Bicelles represent a valuable tool for membrane protein crystallographers.