Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.6K
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.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.6K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.8K
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...
6.8K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

7.0K
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
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

82.7K
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...
82.7K
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...
4.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Evolutionary Engineering a Larger Porin Using a Loop-to-Hairpin Mechanism.

Journal of molecular biology·2023
Same author

Evolutionary engineering a larger porin using a loop-to-hairpin mechanism.

bioRxiv : the preprint server for biology·2023
Same author

Outer membrane protein evolution.

Current opinion in structural biology·2021
Same author

Evolutionary pathways of repeat protein topology in bacterial outer membrane proteins.

eLife·2018

Related Experiment Video

Updated: Mar 11, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

14.0K

Outer membrane protein design.

Joanna Sg Slusky1

  • 1Center for Computational Biology and Department of Molecular Biosciences, University of Kansas, 4010 Haworth Hall, 1200 Sunnyside Ave., Lawrence, KS 66045, United States.

Current Opinion in Structural Biology
|November 29, 2016
PubMed
Summary
This summary is machine-generated.

This review explores the design of outer membrane proteins, which form unique beta-barrels. We categorize designs based on structural deconstruction, changes, chemical function, and novel fold creation.

More Related Videos

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

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

Published on: July 4, 2016

14.2K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.4K

Related Experiment Videos

Last Updated: Mar 11, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

14.0K
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

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

Published on: July 4, 2016

14.2K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Membrane proteins act as cellular gateways and signal transmitters.
  • Outer membrane proteins, found in specific organelles and bacteria, possess a unique beta-barrel structure.
  • Designing these proteins offers potential to harness their biological functions.

Purpose of the Study:

  • To review and categorize known designs of outer membrane beta-barrel proteins.
  • To highlight strategies for engineering these unique protein structures.
  • To explore the potential applications of designed outer membrane proteins.

Main Methods:

  • Literature review of existing outer membrane protein designs.
  • Categorization of designs into four main strategies: structural deconstruction, structural changes, chemical function design, and new fold creation.
  • Analysis of reported examples for each design category.

Main Results:

  • Outer membrane protein design strategies include breaking down existing structures, modifying them, engineering chemical functions, and creating entirely new folds.
  • Numerous examples illustrate the successful application of these design principles.
  • The review provides a comprehensive overview of the current landscape of beta-barrel protein design.

Conclusions:

  • Outer membrane beta-barrel proteins offer a versatile platform for protein design.
  • Understanding and manipulating these structures can lead to novel biotechnological applications.
  • Future research can build upon these design strategies to create advanced protein functionalities.