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

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.4K
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...
5.4K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.9K
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...
6.9K
Amyloid Fibrils03:03

Amyloid Fibrils

13.2K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
13.2K
Amyloid Fibrils03:03

Amyloid Fibrils

7.0K
7.0K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

21.1K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
21.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.8K
15.8K

You might also read

Related Articles

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

Sort by
Same author

Phosphoglycerate Kinase Can Adopt Topologically Misfolded Forms That Are More Stable Than Its Native State.

Journal of the American Chemical Society·2026
Same author

Phosphoglycerate Kinase Can Adopt a Topologically Misfolded Form that is More Stable than its Native State.

bioRxiv : the preprint server for biology·2025
Same author

The lipid bilayer strengthens the cooperative network of membrane proteins.

Science advances·2025
Same author

The molecular basis for hydrodynamic properties of PEGylated human serum albumin.

Biophysical journal·2024
Same author

A team of chaperones play to win in the bacterial periplasm.

Trends in biochemical sciences·2024
Same author

Membrane defects as a generalized driving force for membrane protein interactions.

Proceedings of the National Academy of Sciences of the United States of America·2023

Related Experiment Video

Updated: Apr 19, 2026

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

14.3K

Membrane defects accelerate outer membrane β-barrel protein folding.

Emily J Danoff1, Karen G Fleming

  • 1T. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.

Biochemistry
|December 17, 2014
PubMed
Summary
This summary is machine-generated.

Outer membrane protein folding accelerates in lipid bilayers near their phase transition. This is due to lipid domains and membrane defects, crucial for protein assembly.

More Related Videos

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.9K
Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

12.1K

Related Experiment Videos

Last Updated: Apr 19, 2026

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

14.3K
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.9K
Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

12.1K

Area of Science:

  • Biochemistry
  • Membrane Biology
  • Protein Folding

Background:

  • Outer membrane beta-barrel proteins are essential biological components.
  • Their spontaneous folding into lipid bilayers is vital for cellular function.
  • Membrane physical properties significantly impact protein folding rates.

Purpose of the Study:

  • To investigate the influence of lipid bilayer physical properties on outer membrane beta-barrel protein folding rates.
  • To elucidate the role of membrane defects and phase transitions in protein assembly.

Main Methods:

  • Studied protein folding kinetics in lipid bilayers.
  • Manipulated bilayer physical properties, including temperature and curvature.
  • Analyzed the correlation between membrane defects and folding rates.

Main Results:

  • Protein folding is accelerated at the lipid bilayer's phase transition temperature.
  • The coexistence of lipid phase domains and increased defects at domain boundaries enhances folding.
  • Faster folding was observed in thin and highly curved membranes, which exhibit more defects.

Conclusions:

  • Membrane defects play a critical role in the intrinsic folding process of beta-barrel proteins.
  • Understanding these defects provides insight into the biological assembly pathways of outer membrane proteins.