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Related Concept Videos

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
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...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
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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Updated: May 11, 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

Stabilizing membrane proteins through protein engineering.

Daniel J Scott1, Lutz Kummer, Dirk Tremmel

  • 1The Florey Institute of Neuroscience and Mental Health, The University of Melbourne, Parkville, Victoria 3010, Australia.

Current Opinion in Chemical Biology
|May 4, 2013
PubMed
Summary
This summary is machine-generated.

Integral membrane proteins (IMPs) are essential but challenging to study. This review explores methods like alanine scanning, directed evolution, and computational design to engineer stabilized IMPs for biochemical and structural analysis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Integral membrane proteins (IMPs) are vital cellular components.
  • IMPs are notoriously unstable and difficult to study in vitro when extracted from cell membranes.
  • Less than 1% of Protein Data Bank entries are IMP structures due to these challenges.

Purpose of the Study:

  • To review methods for identifying stabilizing mutations in IMPs.
  • To enable robust biochemical and structural studies of IMPs.
  • To bridge the gap in structural data for IMPs.

Main Methods:

  • Review of techniques for stabilizing IMPs.
  • Discussion of alanine scanning and screening.
  • Exploration of directed evolution and computational design strategies.

Main Results:

  • Stabilizing mutations can be engineered into IMPs.
  • Engineered IMPs can be successfully studied in detergent micelles.
  • Various methods exist for identifying these crucial mutations.

Conclusions:

  • Engineering stability is key to studying IMPs.
  • Multiple approaches are available for identifying stabilizing mutations.
  • Advancements in protein engineering are critical for IMP research.