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Related Concept Videos

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...
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...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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.
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Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Published on: March 5, 2017

Proteins: membrane binding and pore formation. Introduction.

Susanne C Feil1, Galina Polekhina, Michael A Gorman

  • 1St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.

Advances in Experimental Medicine and Biology
|August 7, 2010
PubMed
Summary
This summary is machine-generated.

Pore-forming proteins transform from soluble states to membrane pores through significant shape changes. Recent studies reveal these proteins, like toxins, utilize similar strategies for membrane insertion.

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Pore-forming proteins (PFPs) exhibit dual states: soluble and membrane-integrated.
  • Conformational changes are crucial for PFP function, transitioning between states.
  • Bacterial toxins have been key models for understanding PFP mechanisms.

Purpose of the Study:

  • To explore the conformational changes of pore-forming proteins.
  • To investigate the strategies PFPs use for membrane binding and insertion.
  • To compare PFP mechanisms with those of known toxins.

Main Methods:

  • Characterization of recently identified pore-forming proteins.
  • Analysis of protein structures and conformational dynamics.
  • Comparative studies with bacterial toxins.

Main Results:

  • PFPs undergo substantial conformational changes to form membrane pores.
  • Emerging evidence shows non-toxin PFPs employ toxin-like strategies for membrane interaction.
  • Similarities in binding and insertion mechanisms are observed across diverse PFPs.

Conclusions:

  • Pore-forming proteins utilize conserved mechanisms for membrane insertion, similar to toxins.
  • Understanding these conformational changes offers insights into protein function and potential therapeutic targets.
  • The study highlights convergent evolution in protein structure-function relationships.