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 Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
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...
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...

You might also read

Related Articles

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

Sort by
Same author

[Y97V substitution in the horse cytochrome c causes accumulation of the equilibrium intermediate].

Biofizika·2001
Same author

Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins.

Biochemistry·2000
Same author

[Self-organization of protein structures--a bridge between physics and biology].

Molekuliarnaia biologiia·2000
Same author

Non-functional conserved residues in globins and their possible role as a folding nucleus.

Journal of molecular biology·1999
Same author

Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin.

FEBS letters·1999
Same author

Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin.

Protein engineering·1999

Related Experiment Video

Updated: May 28, 2026

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

Protein folding: nucleation and compact intermediates

O B Ptitsyn1

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia. ptitsyn@sun.ipr.serpukhov. su

Biochemistry. Biokhimiia
|April 29, 1998
PubMed
Summary
This summary is machine-generated.

Protein folding research reveals basic principles. Two-state folding involves a nucleus, while complex folding may use a nucleus in the transition state to a compact intermediate.

More Related Videos

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Related Experiment Videos

Last Updated: May 28, 2026

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

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Dynamics and Folding

Background:

  • Understanding protein folding is crucial for molecular biology.
  • Protein folding can occur via simple two-state transitions or more complex pathways involving intermediates.

Purpose of the Study:

  • To elucidate the fundamental principles governing protein folding.
  • To explore the role of the folding nucleus in different folding pathways.

Main Methods:

  • Combines experimental studies with theoretical modeling.
  • Investigates the formation and growth of the folding nucleus.

Main Results:

  • Identified basic principles of protein folding.
  • Characterized two-state folding initiated by a folding nucleus.
  • Observed that complex folding often proceeds via a compact intermediate with native-like features.

Conclusions:

  • The folding nucleus plays a key role in initiating protein folding.
  • In complex folding pathways, the folding nucleus may be involved in the transition state leading to compact intermediates.