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

9.2K
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...
9.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.6K
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...
18.6K
Protein Organization01:13

Protein Organization

147.3K
Overview
147.3K
Improving Translational Accuracy02:07

Improving Translational Accuracy

11.9K
Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
11.9K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

122
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
122
Protein and Protein Structure02:15

Protein and Protein Structure

82.3K
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...
82.3K

You might also read

Related Articles

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

Sort by
Same author

Coexistence of two coacervate phases of polyglycine in water suggested by polymer reference interaction site model theory.

The Journal of chemical physics·2023
Same author

Effects of intramolecular chain conformation on the hydration and miscibility of polyethylene glycol in water studied by means of polymer reference interaction site model theory.

The Journal of chemical physics·2023
Same author

Phase equilibrium of three-component liquid systems composed of water, alcohol, and sodium chloride studied by the reference interaction-site model integral equation theory.

The Journal of chemical physics·2023
Same author

Evolutionary conservation of amino acids contributing to the protein folding transition state.

Journal of computational chemistry·2022
Same author

Atomic-level thermodynamics analysis of the binding free energy of SARS-CoV-2 neutralizing antibodies.

Proteins·2022
Same author

Study of phase equilibria and thermodynamic properties of liquid mixtures using the integral equation theory: Application to water and alcohol mixtures.

The Journal of chemical physics·2022

Related Experiment Video

Updated: Sep 28, 2025

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

15.2K

Time-dependent communication between multiple amino acids during protein folding.

Song-Ho Chong1, Sihyun Ham1

  • 1Department of Chemistry, The Research Institute of Natural Sciences, Sookmyung Women's University Cheongpa-ro-47-gil 100, Yongsan-ku Seoul 04310 Korea sihyun@sookmyung.ac.kr.

Chemical Science
|March 28, 2022
PubMed
Summary

Protein folding cooperativity, crucial for biomolecular processes, is quantified using multipoint time-correlation functions. The study reveals maximal amino acid cooperativity at the transition state, offering new insights into protein folding mechanisms.

More Related Videos

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

18.4K
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

Related Experiment Videos

Last Updated: Sep 28, 2025

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

15.2K
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

18.4K
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

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Dynamics

Background:

  • Cooperativity is fundamental to biomolecular assembly, recognition, and folding.
  • Quantifying cooperative processes on a molecular, multi-interaction basis remains challenging.

Purpose of the Study:

  • To investigate the molecular-scale mechanisms and timing of protein folding cooperativity.
  • To develop a quantitative method for characterizing multi-interaction cooperativity during folding.

Main Methods:

  • Analysis of multipoint time-correlation functions from long folding simulation trajectories.
  • Probing time-dependent communication between multiple amino acids.

Main Results:

  • Simultaneous multiple amino acid contact formation emerges during the folding transition path.
  • Maximal amino acid cooperativity is observed at the protein folding transition state.
  • This transition state is linked to cooperative behavior in two-state folding.

Conclusions:

  • Provides a novel mechanistic understanding of protein folding based on multiple interactions.
  • Offers a new characterization of the folding transition state and the origin of cooperative folding.
  • The multipoint correlation function approach is applicable to other complex biomolecular systems.