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

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 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...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

You might also read

Related Articles

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

Sort by
Same author

Acid Versus Amide-Facts and Fallacies: A Case Study in Glycomimetic Ligand Design.

Molecules (Basel, Switzerland)·2025
Same author

A multichaperone condensate enhances protein folding in the endoplasmic reticulum.

Nature cell biology·2025
Same author

Architecture and conformational dynamics of the BAM-SurA holo insertase complex.

Science advances·2025
Same author

Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process.

Biomolecules·2025
Same author

The carbonyl nucleobase adduct M<sub>3</sub>Ade is a potent antigen for adaptive polyclonal MR1-restricted T cells.

Immunity·2024
Same author

Strengthening an Intramolecular Non-Classical Hydrogen Bond to Get in Shape for Binding.

Angewandte Chemie (International ed. in English)·2024

Related Experiment Video

Updated: Jul 6, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Energetic coupling between native-state prolyl isomerization and conformational protein folding.

Roman P Jakob1, Franz X Schmid

  • 1Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, D-95440 Bayreuth, Germany.

Journal of Molecular Biology
|March 8, 2008
PubMed
Summary

Proline isomerization in proteins is crucial for folding. This study reveals that the N2 domain of phage fd gene-3 protein accommodates both cis and trans proline isomers, with folding energy driving this equilibrium.

More Related Videos

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Related Experiment Videos

Last Updated: Jul 6, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Area of Science:

  • Protein folding and dynamics
  • Biophysics
  • Molecular biology

Background:

  • Prolyl peptide bonds typically exist as either trans or cis isomers in folded proteins.
  • The N-terminal domain of gene-3 protein (N2 domain) from filamentous phage fd features Pro161 at a beta hairpin tip, previously observed in the cis conformation.

Purpose of the Study:

  • To investigate the coupling between conformational folding and prolyl isomerization in the N2 domain.
  • To determine if Pro161 exists in both cis and trans conformations in the folded N2 domain.
  • To elucidate the kinetics and thermodynamics of Pro161 isomerization during protein folding.

Main Methods:

  • Utilized single-mixing and double-mixing unfolding and refolding experiments.
  • Analyzed the cis/trans equilibrium of Pro161 during refolding.
  • Applied a four-species box model to describe folding kinetics.

Main Results:

  • In the unfolded N2 domain, 7% of molecules have cis-Pro161 and 93% have trans-Pro161.
  • During refolding, the fraction of cis-Pro161 increases to 85%, indicating a 75-fold change in equilibrium.
  • Folding free energy of 10.3 kJ mol(-1) drives this isomerization equilibrium shift.
  • Conformational folding is faster than prolyl isomerization, allowing separate determination of isomer stabilities and folding kinetics.
  • Energetic coupling between folding and isomerization is established in the folding transition state.

Conclusions:

  • Pro161 exists in both cis and trans conformations in the folded N2 domain, challenging the notion of a single native isomer.
  • The folding process actively drives the Pro161 cis/trans equilibrium towards the cis isomer.
  • Both cis and trans isomers represent native forms, with cis/trans isomerization occurring in both unfolded and folded states.