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Related Concept Videos

Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Multi-pass Transmembrane Proteins and β-barrels01:09

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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
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Single-pass Transmembrane Proteins01:25

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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...
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Structure of Porins01:21

Structure of Porins

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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...
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Membrane Proteins01:30

Membrane Proteins

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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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Related Experiment Video

Updated: Nov 20, 2025

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

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Outer membrane protein evolution.

Rik Dhar1, Joanna Sg Slusky2

  • 1Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Ave., Lawrence KS 66045-3101, United States.

Current Opinion in Structural Biology
|January 25, 2021
PubMed
Summary
This summary is machine-generated.

Outer membrane proteins feature a consistent beta-barrel structure, built from repeating beta-hairpins. This structural uniformity enables the study of their evolution and the design of new proteins.

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Area of Science:

  • Structural biology
  • Evolutionary biology
  • Protein engineering

Background:

  • Outer membrane proteins (OMPs) exhibit a conserved "up-down" beta-barrel structure.
  • This structure is composed of repeating beta-hairpin units.
  • The repetitive nature of OMPs facilitates evolutionary analysis.

Purpose of the Study:

  • To investigate the evolutionary pathways of outer membrane protein structures.
  • To explore the application of evolutionary principles in designing novel OMPs.

Main Methods:

  • Analysis of conserved structural motifs in outer membrane proteins.
  • Comparative studies of beta-hairpin repetition and evolution.
  • Computational and experimental approaches for protein design based on evolutionary insights.

Main Results:

  • Demonstration of the evolutionary consistency of beta-hairpin usage in OMPs.
  • Identification of key evolutionary pressures shaping OMP structure.
  • Successful application of evolutionary precepts for novel OMP design.

Conclusions:

  • The homogeneous structure of outer membrane proteins provides a unique system for studying molecular evolution.
  • Evolutionary insights can be effectively leveraged to engineer new protein functions and structures.