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

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

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

You might also read

Related Articles

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

Sort by

Same author

Single-molecule fluorescence spectroscopy and imaging of heterogeneous amyloid β aggregation.

Methods in enzymology·2026

Same author

Cooperative Native Contact Formation Facilitates Free Energy Barrier Crossing in Protein Folding.

Physical review letters·2026

Same author

Long-term mitapivat treatment is safe and efficacious in patients with sickle cell disease.

Blood. Red cells & iron·2026

Same author

Dynamic control of IDP interaction network via diverse binding pathways.

Nature communications·2026

Same author

Pyruvate kinase deficiency modifies sickle hemoglobin carrier and sickle cell disease phenotypes in mice.

JCI insight·2026

Same author

Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.

PNAS nexus·2025

Search research articles

Related Experiment Video

Updated: Apr 3, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Structural origin of slow diffusion in protein folding.

Hoi Sung Chung¹, Stefano Piana-Agostinetti², David E Shaw³

¹Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA. chunghoi@niddk.nih.gov stefano.piana-agostinetti@DEShawResearch.com david.shaw@DEShawResearch.com eaton@helix.nih.gov.

Science (New York, N.Y.)

|September 26, 2015

Summary

Non-native salt bridges between helices slow protein folding by hindering diffusion, not by altering free energy barriers. This study reveals how specific intramolecular interactions impact protein dynamics and folding rates.

More Related Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

Related Experiment Videos

Last Updated: Apr 3, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

Area of Science:

Biophysics
Computational Biology
Protein Dynamics

Background:

Small protein self-assembly is generally independent of non-native contacts.
Non-native contacts can impede protein folding kinetics by creating local energy minima.

Purpose of the Study:

Investigate the structural basis for slow diffusion in a designed alpha-helical protein.
Determine how intramolecular interactions affect protein folding rates.

Main Methods:

Single-molecule fluorescence experiments
All-atom molecular dynamics simulations
Transition path time analysis

Main Results:

Identified non-native salt bridges between helices as the cause of slow diffusion.
Demonstrated that these interactions alter protein dynamics.
Showed that folding rates are influenced by dynamics, not activation free energies.

Conclusions:

Non-native salt bridges significantly impact protein folding kinetics.
Intramolecular interactions can modulate protein folding through dynamic effects rather than free energy changes.