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Related Concept Videos

Structure of Porins01:21

Structure of Porins

4.1K
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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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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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
Multi-pass transmembrane proteins such as...
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Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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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...
7.0K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.1K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.2K
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...
19.2K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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Updated: Mar 14, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Engineered transmembrane pores.

Mariam Ayub1, Hagan Bayley1

  • 1Department of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom.

Current Opinion in Chemical Biology
|September 23, 2016
PubMed
Summary
This summary is machine-generated.

Researchers are engineering novel protein nanopores for biotechnology applications. New designs include helix-based, truncated, and hybrid pores, expanding possibilities beyond DNA sequencing.

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Engineering Cell-permeable Protein
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Last Updated: Mar 14, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Engineering Cell-permeable Protein
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Area of Science:

  • Biotechnology
  • Biophysics
  • Materials Science

Background:

  • Nanopores, particularly protein-based ones, are crucial tools in basic science and biotechnology.
  • Engineering proteins with sub-nanometer precision enables versatile nanopore applications.

Purpose of the Study:

  • To review recent advancements in the construction and discovery of novel nanopores.
  • To highlight the expanding structural diversity and potential applications of engineered nanopores.

Main Methods:

  • Unnatural amino acid mutagenesis for novel pore construction.
  • Selection techniques for discovering new nanopore structures.
  • Development of helix-based pores and beta-barrels.
  • Engineering of truncated, hybrid, and pore dimer structures.
  • Construction of DNA nanostructure-based pores.

Main Results:

  • Increased structural diversity with helix-based and beta-barrel pores.
  • Development of truncated pores that utilize lipid rearrangement.
  • Creation of hybrid pores that eliminate the need for bilayers.
  • Construction of pore dimers spanning two lipid bilayers.
  • Growing importance of DNA nanostructure-based pores.

Conclusions:

  • Protein nanopores offer a wider range of applications than DNA sequencing.
  • Continued engineering efforts are required to meet future application specifications.
  • Nanopore research is a dynamic field with ongoing innovation in structure and function.