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 Folding01:25

Protein Folding

8.3K
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...
8.3K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.2K
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...
18.2K
Amyloid Fibrils03:03

Amyloid Fibrils

9.7K
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,...
9.7K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.1K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.1K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
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...
3.8K
Protein and Protein Structure02:15

Protein and Protein Structure

80.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
80.0K

You might also read

Related Articles

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

Sort by
Same author

Sign Epistasis Can be Absent in Multi-peaked Landscapes With Neutral Mutations.

Genome biology and evolution·2026
Same author

MPXV RNA-seq data provide evidence for protection of viral transcripts from APOBEC3 editing.

Journal of virology·2026
Same author

Tracking Down the Evolution of Microorganisms by Exhaustive Bottom-Up Analysis of Proteomes.

International journal of molecular sciences·2026
Same author

KRASAVA-An Expert System for Virtual Screening of KRAS G12D Inhibitors.

International journal of molecular sciences·2026
Same author

Convergent pairs of highly transcribed genes restrict chromatin looping in Dictyostelium discoideum.

Nucleic acids research·2025
Same author

How proteins manage to fold and how chaperones manage to assist the folding.

Physics of life reviews·2024
Same journal

Navigating the labyrinth of drugging the disordered.

Biophysical reviews·2026
Same journal

<i>Biophysical Reviews</i>: a forum for publication of review articles from the international biophysics community.

Biophysical reviews·2026
Same journal

Mitochondrial potassium channels: mitochondria-specific mechanism of regulation.

Biophysical reviews·2026
Same journal

Biomolecular condensates in living systems: from function to disease. What to do next.

Biophysical reviews·2026
Same journal

Astrocyte morphology: complex or trivial?

Biophysical reviews·2026
Same journal

Correction to: A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributions.

Biophysical reviews·2026
See all related articles

Related Experiment Video

Updated: Aug 13, 2025

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

18.4K

Protein folding problem: enigma, paradox, solution.

Alexei V Finkelstein1,2,3, Natalya S Bogatyreva1, Dmitry N Ivankov4

  • 1Institute of Protein Research of the Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.

Biophysical Reviews
|January 20, 2023
PubMed
Summary
This summary is machine-generated.

Protein folding kinetics explains how protein chains find their functional 3D structures rapidly, resolving Levinthal's paradox. Modern theories align with experiments, predicting folding times and maximal protein sizes.

Keywords:
Folding funnelFree energy landscapeLevinthal’s paradoxProtein 3D structureProtein folding“All-or-none” phase transition

More Related Videos

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

12.9K
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

11.3K

Related Experiment Videos

Last Updated: Aug 13, 2025

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

18.4K
Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

12.9K
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

11.3K

Area of Science:

  • Molecular Biology
  • Biophysics
  • Biochemistry

Background:

  • Protein chains must achieve specific 3D structures for function.
  • The spontaneous folding process faces Levinthal's paradox: an impossibly long time to explore all conformations.
  • Understanding protein folding kinetics is crucial for molecular biology.

Purpose of the Study:

  • To review key discoveries in protein folding kinetics.
  • To explain the resolution of Levinthal's paradox.
  • To present the modern theoretical understanding of protein folding.

Main Methods:

  • Discussion of folding landscapes and funnels.
  • Analysis of free energy barriers in folding/unfolding pathways.
  • Examination of 'all-or-none' phase transitions and thermodynamic equilibrium.

Main Results:

  • Modern theory explains key protein folding features.
  • Predictions align with experimental data on folding times and maximal protein sizes.
  • The theory distinguishes between thermodynamic and kinetic control in protein folding.

Conclusions:

  • The current understanding of protein folding kinetics, including landscapes and phase transitions, resolves Levinthal's paradox.
  • Theoretical models accurately predict folding times and the maximum size of foldable proteins.
  • Protein folding is understood through a combination of thermodynamic and kinetic principles.