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

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Protein Folding01:22

Protein Folding

Overview
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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...

You might also read

Related Articles

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

Sort by
Same author

Distinct mechanistic pathways of early tauopathy revealed by <i>MAPT</i> mutations.

bioRxiv : the preprint server for biology·2026
Same author

The impact of physical activity and intensity on clot mechanical microstructure and contraction in middle-aged/older habitual runners.

BMC neurology·2025
Same author

Exercise transiently increases the density of incipient blood clots in antiplatelet-treated lacunar stroke patients.

Thrombosis journal·2024
Same author

The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

The treatment effect of rivaroxaban on clot characteristics in patients who present acutely with first time deep vein thrombosis.

Clinical hemorheology and microcirculation·2021
Same author

The effect of the acute inflammatory response of burns and its treatment on clot characteristics and quality: A prospective case controlled study.

Burns : journal of the International Society for Burn Injuries·2019

Related Experiment Video

Updated: Jul 6, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

The folding of hen lysozyme involves partially structured intermediates and multiple pathways.

S E Radford1, C M Dobson, P A Evans

  • 1Oxford Centre for Molecular Sciences, University of Oxford, UK.

Nature
|July 23, 1992
PubMed
Summary

Hen lysozyme protein folding is not a single event. Different protein regions stabilize at distinct rates, with alpha-helical domains folding faster than beta-sheet domains.

More Related Videos

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Related Experiment Videos

Last Updated: Jul 6, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Dynamics

Background:

  • Protein folding is crucial for biological function.
  • Understanding folding pathways provides insights into protein structure and stability.
  • Hen lysozyme is a model protein for studying folding mechanisms.

Purpose of the Study:

  • To analyze the folding kinetics of hen lysozyme.
  • To determine if protein folding occurs as a single cooperative event.
  • To investigate the presence of distinct folding pathways.

Main Methods:

  • Kinetic analysis of hen lysozyme folding.
  • Differential stabilization rates of protein domains.
  • Identification of kinetically distinct molecular populations.

Main Results:

  • Hen lysozyme folding is not a single cooperative event.
  • Alpha-helical and beta-sheet domains exhibit different folding kinetics.
  • Multiple, distinct folding pathways are utilized by different molecule populations.
  • Some folding pathways involve significant molecular reorganization.

Conclusions:

  • Protein folding is a complex process involving parallel pathways.
  • Folding kinetics vary across different regions of the protein.
  • Alternative folding pathways contribute to the overall folding process.