Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Molecular Chaperones and Protein Folding

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 Folding

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 Folding

Protein Folding

Protein Folding

Protein Folding

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Protein and Protein Structure

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...

You might also read

Related Articles

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

Sort by

Same author

Solvent-Mediated Control of Nanocellulose Dispersion: An Integrated Computational and Experimental Investigation.

ACS nano·2026

Same author

Water-modulated conformational heterogeneity underlies multiple timescales of primary charge separation in photosystem II.

Nature communications·2026

Same author

A general hydrogen-bond connectivity descriptor based on graph theory.

Physical chemistry chemical physics : PCCP·2026

Same author

The scientific legacy of Martin Karplus from the perspective of his collaborators.

Biophysical journal·2026

Same author

IRIS: A Machine Learning-Based Pose Reranking Tool for RNA-Ligand Docking.

ACS omega·2026

Same author

Interaction of a porphyrinic cage with ethionamide: a spectroscopic and computational study.

Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology·2026

Same journal

DeepMethylation: A deep learning framework for tissue-specific DNA methylation prediction and functional variant annotation.

PLoS computational biology·2026

Same journal

Redefining and estimating the early-phase reproduction ratio for epidemic outbreaks in spatially structured populations.

PLoS computational biology·2026

Same journal

Optimized phenotype definitions boost GWAS power.

PLoS computational biology·2026

Same journal

Detection, communication, and individual identification with deep audio embeddings: A case study with North Atlantic right whales.

PLoS computational biology·2026

Same journal

Exploring the structural lexicon of the Proteome via Metric Geometry.

PLoS computational biology·2026

Same journal

Linking retinal sampling in neural encoding models to temporal profiles of visual processing in humans.

PLoS computational biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 16, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.

Isabella Daidone¹, Hannes Neuweiler, Sören Doose

¹Interdisciplinary Center for Scientific Computing, University of Heidelberg, Heidelberg, Germany. Isabella.Daidone@iwr.uni-heidelberg.de

Plos Computational Biology

|January 26, 2010

Summary

This summary is machine-generated.

Protein folding kinetics in unfolded peptides depend on chain length. Hydrogen bonds and beta-sheet structures accelerate contact formation in longer chains, aiding protein folding.

More Related Videos

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Studying DNA Looping by Single-Molecule FRET

Studying DNA Looping by Single-Molecule FRET

Published on: June 28, 2014

Related Experiment Videos

Last Updated: Jun 16, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Studying DNA Looping by Single-Molecule FRET

Studying DNA Looping by Single-Molecule FRET

Published on: June 28, 2014

Area of Science:

Biophysics
Computational Biology
Protein Science

Background:

Understanding protein folding is crucial for molecular biology.
Early steps in protein folding involve loop-closure kinetics.
Polypeptide chain dynamics influence protein structure formation.

Purpose of the Study:

To investigate the length dependence of end-to-end loop-closure kinetics in unfolded polypeptide chains.
To understand the role of hydrogen bonds and secondary structures in protein folding.
To explore the impact of experimental conditions on folding kinetics.

Main Methods:

Single-molecule fluorescence spectroscopy was used to monitor loop-closure.
Molecular dynamics simulations provided insights into peptide chain behavior.
Poly-glycine-serine peptides were used as model systems.

Main Results:

Loop-closing rate constants exhibit a power-law length dependence for peptides longer than 10 peptide bonds.
Shorter peptides showed slower kinetics due to experimental dye perturbation.
Intra-peptide hydrogen bonds and transient beta-sheet structures accelerate contact formation in longer chains.

Conclusions:

Hydrogen-bond-driven collapse in unfolded peptides is consistent with hierarchical protein folding models.
Secondary structure formation plays a key role in early folding events.
This process speeds up the search for productive folding pathways.