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Related Concept Videos

Protein Diffusion in the Membrane01:24

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...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
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...

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Related Experiment Video

Updated: Jun 16, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

New tools for membrane protein research.

Yilmaz Alguel1, James Leung, Shweta Singh

  • 1Division of Molecular Biosciences, Imperial College London, South Kensington, London, SW7 2AZ, UK.

Current Protein & Peptide Science
|January 22, 2010
PubMed
Summary
This summary is machine-generated.

Advancing eukaryotic membrane protein structural studies requires novel techniques. Recent high-throughput methods, including GFP fusions and mutant screening, improve structural characterization of these vital proteins.

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Last Updated: Jun 16, 2026

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High-Throughput Expression and Purification of Human Solute Carriers for Structural and Biochemical Studies

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Significant increase in membrane protein structures determined recently.
  • Majority of solved structures are prokaryotic, limiting understanding of eukaryotic proteins.
  • High-resolution structural data for clinically relevant eukaryotic membrane proteins is scarce.

Purpose of the Study:

  • To review novel techniques for eukaryotic membrane protein structural characterization.
  • To highlight recent advancements impacting structural biology approaches.
  • To address the need for improved methods in determining eukaryotic membrane protein structures.

Main Methods:

  • Review of recently developed high-throughput techniques.
  • Screening membrane proteins using Green Fluorescent Protein (GFP) fusions.
  • Generating protein mutants to enhance stability and facilitate crystallization.

Main Results:

  • Identification of high-throughput strategies for selecting suitable membrane proteins.
  • Development of methods to produce stable, well-diffracting eukaryotic membrane proteins.
  • Recent techniques are significantly impacting the approach to structural studies.

Conclusions:

  • Novel techniques are crucial for advancing eukaryotic membrane protein structural biology.
  • High-throughput screening and protein engineering are key strategies.
  • These advancements promise to increase the availability of structural data for important eukaryotic proteins.