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

9.5K
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...
9.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.7K
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...
18.7K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.6K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.6K
Protein Organization01:13

Protein Organization

149.5K
Overview
149.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.1K
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...
13.1K
Protein and Protein Structure02:15

Protein and Protein Structure

82.9K
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...
82.9K

You might also read

Related Articles

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

Sort by
Same author

The master molecule that built biology: How water shaped the chemistry of life.

Protein science : a publication of the Protein Society·2026
Same author

50 years in the shadow of the Ramachandran plot.

Protein science : a publication of the Protein Society·2025
Same author

From propensities to patterns to principles in protein folding.

Proteins·2023
Same author

Opinion: Protein folds vs. protein folding: Differing questions, different challenges.

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

Protein folding - seeing is deceiving.

Protein science : a publication of the Protein Society·2021
Same author

Ramachandran maps for side chains in globular proteins.

Proteins·2019
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
Same journal

Structural Bases for the Unconventional Activity of a Viroporin Channel.

Biochemistry·2026
Same journal

Targeting the WASF3 Regulatory Complex in Pancreatic Cancer Using Stapled Peptides.

Biochemistry·2026
Same journal

Thermodynamic and Allosteric Drivers of Stilbene-Mediated Noncompetitive Inhibition of Firefly Luciferase.

Biochemistry·2026
See all related articles

Related Experiment Video

Updated: Oct 11, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K

Reframing the Protein Folding Problem: Entropy as Organizer.

George D Rose1

  • 1T. C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218-2683, United States.

Biochemistry
|December 2, 2021
PubMed
Summary
This summary is machine-generated.

Protein folding is driven by conformational entropy, not just enthalpy. Satisfying backbone hydrogen bonds is thermodynamically essential, guiding proteins to form stable structures like alpha-helices and beta-sheets.

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K
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

9.2K

Related Experiment Videos

Last Updated: Oct 11, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K
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

9.2K

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Structural Biology

Background:

  • The traditional view posits protein folding is driven by enthalpic interactions.
  • This perspective challenges that, highlighting the role of conformational entropy.

Purpose of the Study:

  • To introduce a novel mechanism for protein folding emphasizing conformational entropy.
  • To explain how hydrogen bond satisfaction dictates protein structure.

Main Methods:

  • Theoretical analysis of thermodynamic principles.
  • Examination of protein folding pathways and conformational landscapes.

Main Results:

  • Backbone hydrogen bond satisfaction is a critical thermodynamic driver.
  • Unsatisfied hydrogen bonds are highly destabilizing, favoring folded states.
  • Alpha-helices and beta-sheets are favored scaffolds due to balanced hydrogen bonding.

Conclusions:

  • Conformational entropy, through hydrogen bond satisfaction, is the principal organizer of protein folding.
  • This mechanism explains the selection of native protein structures and allows for evolutionary adaptation.