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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

You might also read

Related Articles

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

Sort by
Same author

Environmental Identification of Novel Enzymes for Polyurethane and Polyamide Degradation.

Angewandte Chemie (International ed. in English)·2026
Same author

Double-Stranded DNA Sensing cGAS-STING Immune Signaling in a Rat Co-Culture Model of the Blood-Brain Barrier.

Cell biochemistry and function·2026
Same author

Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Mechanism-selective inhibition of α-synuclein aggregation by the chaperone-like BRICHOS domain.

The Journal of biological chemistry·2026
Same author

Exosomes as Advanced Nanocarriers: Overcoming the Blood-Brain Barrier for Targeted Therapeutic Delivery in Neurodegenerative Diseases.

Current drug delivery·2026
Same author

When motion slows: intrinsic photophysics of thioflavin T and X cations at cryogenic temperatures.

Physical chemistry chemical physics : PCCP·2026

Related Experiment Video

Updated: May 17, 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

Folding of outer membrane proteins.

Daniel E Otzen1, Kell K Andersen

  • 1Interdisciplinary Nanoscience Center (iNANO), Center for Insoluble Protein Structures (inSPIN), Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark. dao@inano.au.dk

Archives of Biochemistry and Biophysics
|November 8, 2012
PubMed
Summary

Outer membrane proteins (OMPs) are valuable models for studying protein folding in membranes. Optimized conditions and surfactant use enable detailed kinetic analysis of OMP folding and unfolding.

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

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

Related Experiment Videos

Last Updated: May 17, 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

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

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

Area of Science:

  • Membrane protein biophysics
  • Protein folding dynamics
  • Structural biology

Background:

  • Outer membrane proteins (OMPs) are beta-barrel proteins crucial in bacterial and eukaryotic membranes.
  • Their accessibility for expression and refolding makes them ideal models for studying membrane protein folding.
  • Understanding OMP folding is key to deciphering membrane insertion and biological function.

Purpose of the Study:

  • To review in vitro methods for studying OMP folding and unfolding.
  • To highlight challenges and recent advancements in achieving reversible OMP folding.
  • To explore the kinetics of OMP folding and unfolding mechanisms.

Main Methods:

  • In vitro refolding and unfolding assays.
  • Use of optimized buffer conditions (e.g., extreme pH, short-chain phospholipids).
  • Surfactant-mediated solubilization for kinetic studies.
  • Protein engineering approaches for high-resolution mechanism elucidation.

Main Results:

  • Rigorous optimization allows for reversible OMP folding, minimizing hysteresis.
  • Surfactants provide a viable alternative for studying OMP unfolding kinetics, even for kinetically stable proteins.
  • Protein engineering offers potential for atomic-level resolution of OMP folding mechanisms.

Conclusions:

  • Studying OMPs in vitro provides valuable insights into membrane protein folding pathways.
  • Advancements in experimental conditions and techniques are crucial for accurate kinetic analysis.
  • Integrating folding insights with membrane environment complexity opens new avenues in membrane protein science.