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

Protein Folding01:22

Protein Folding

112.2K
Overview
112.2K
Protein Folding01:25

Protein Folding

8.7K
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...
8.7K
Protein Folding01:22

Protein Folding

29.7K
29.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.7K
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...
14.7K
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

2.6K
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
2.6K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.2K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.2K

You might also read

Related Articles

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

Sort by
Same author

Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy.

Quarterly reviews of biophysics·2021
Same author

BAmSA: Visualising transmembrane regions in protein complexes using biotinylated amphipols and electron microscopy.

Biochimica et biophysica acta. Biomembranes·2018
Same author

Co-delivery of amphipol-conjugated adjuvant with antigen, and adjuvant combinations, enhance immune protection elicited by a membrane protein-based vaccine against a mucosal challenge with Chlamydia.

Vaccine·2018
Same author

Folding and stabilizing membrane proteins in amphipol A8-35.

Methods (San Diego, Calif.)·2018
Same author

Membranes Do Not Tell Proteins How To Fold.

Biochemistry·2015
Same author

Synthesis of a Polyhistidine-bearing Amphipol and its Use for Immobilizing Membrane Proteins.

Biomacromolecules·2015

Related Experiment Video

Updated: Apr 27, 2026

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

17.5K

Folding membrane proteins in vitro: a table and some comments.

Jean-Luc Popot1

  • 1Centre National de la Recherche Scientifique/Université Paris-7 UMR 7099, Institut de Biologie Physico-Chimique (FRC 550), 13, rue Pierre-et-Marie-Curie, F-75005 Paris, France.

Archives of Biochemistry and Biophysics
|July 6, 2014
PubMed
Summary

In vitro refolding of membrane proteins (MPs) is feasible and improving. Many MPs can achieve functional structures without cellular machinery or membranes, encouraging new experimental approaches.

Keywords:
BiochemistryBiophysicsFoldingMembrane proteinsSurfactants

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

12.6K
In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

14.0K

Related Experiment Videos

Last Updated: Apr 27, 2026

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

17.5K
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

12.6K
In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

14.0K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • Membrane proteins (MPs) are crucial for cellular functions but challenging to study.
  • In vitro refolding of denatured MPs to their native state has been pursued for over three decades.
  • This process is often perceived as difficult, time-consuming, and with a low success rate.

Purpose of the Study:

  • To analyze the literature on in vitro refolding of membrane proteins.
  • To demonstrate that in vitro refolding of MPs is a viable and increasingly successful technique.
  • To provide a compilation of successfully refolded MPs and their conditions to guide future research.

Main Methods:

  • Literature review and compilation of reported in vitro refolding experiments for membrane proteins.
  • Analysis of synthesis conditions, denaturants used, and refolding protocols.
  • Categorization of membrane proteins based on their refolding success and requirements.

Main Results:

  • A significant number of membrane proteins have been successfully refolded in vitro.
  • Techniques for in vitro refolding are diversifying and improving.
  • Many membrane proteins can achieve their functional 3D structure without cellular biosynthesis or a membrane environment.

Conclusions:

  • In vitro refolding of membrane proteins is a more accessible and reliable technique than previously thought.
  • The findings encourage biochemists to consider in vitro refolding for membrane protein production and study.
  • Further research into favorable environments for membrane protein folding is warranted.