Jove
Visualize
Contact Us

Related Concept Videos

Protein Folding01:25

Protein Folding

9.8K
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...
9.8K
Protein Folding01:22

Protein Folding

123.9K
Overview
123.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.8K
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...
18.8K
Termination of Translation01:44

Termination of Translation

26.4K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
26.4K
Protein Organization01:13

Protein Organization

151.3K
Overview
151.3K
Protein Organization01:24

Protein Organization

8.1K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
8.1K

You might also read

Related Articles

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

Sort by
Same author

A Simple Doublet Lens Design for Mid-Infrared Imaging.

Applied spectroscopy·2024
Same author

β-Bracelets: Macrocyclic Cross-β Epitope Mimics Based on a Tau Conformational Strain.

Journal of the American Chemical Society·2023
Same author

Epithelial NAD<sup>+</sup> depletion drives mitochondrial dysfunction and contributes to intestinal inflammation.

Frontiers in immunology·2023
Same author

Cross-α/β polymorphism of PSMα3 fibrils.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

Local Electric Fields in Aqueous Electrolytes.

The journal of physical chemistry. B·2021
Same author

Hydrogen Bond Exchange and Ca<sup>2+</sup> Binding of Aqueous <i>N</i>-Methylacetamide Revealed by 2DIR Spectroscopy.

The journal of physical chemistry. B·2020
Same journal

From cyclic diaryl λ<sup>3</sup>-bromanes/chloranes to polyfuntionalized biarylsilanes <i>via</i> aryne σ-bonds.

Chemical science·2026
Same journal

Non-equilibrium formation of the elusive dibridged diboranyl (B<sub>2</sub>H<sub>5</sub>) radical and boranes in low-temperature diborane ices.

Chemical science·2026
Same journal

Visible-light-driven ruthenium-catalyzed hydrogenation of manganese nitride complexes to ammonia under ambient conditions.

Chemical science·2026
Same journal

Quantification of mesopore infiltration in a polymer-grafted metal-organic framework.

Chemical science·2026
Same journal

Enhanced and selective oxygen reduction by iron porphyrin with a biguanide residue in the second coordination sphere.

Chemical science·2026
Same journal

Excited-state orbital angular momentum enables all-optical molecular spin coherence.

Chemical science·2026
See all related articles
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 Experiment Video

Updated: Nov 1, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.1K

Does liquid-liquid phase separation drive peptide folding?

Dean N Edun1, Meredith R Flanagan1, Arnaldo L Serrano1

  • 1Department of Chemistry and Biochemistry, University of Notre Dame Notre Dame Indiana 46556 USA arnaldo.serrano@nd.edu.

Chemical Science
|June 24, 2021
PubMed
Summary
This summary is machine-generated.

Proline-arginine dipeptide repeats form liquid droplets, concentrating proteins and potentially causing disease. These droplets induce the peptides to fold into poly-proline helical structures, influencing protein aggregation.

More Related Videos

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
04:25

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach

Published on: August 8, 2025

1.0K
In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

Published on: June 28, 2019

5.9K

Related Experiment Videos

Last Updated: Nov 1, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.1K
Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
04:25

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach

Published on: August 8, 2025

1.0K
In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

Published on: June 28, 2019

5.9K

Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) can undergo liquid-liquid phase separation (LLPS).
  • IDP-rich membraneless organelles are implicated in pathogenic protein aggregation.
  • Proline-arginine (PR) dipeptide repeats are a model system for studying LLPS in IDPs.

Purpose of the Study:

  • To investigate the effect of LLPS on peptide secondary structure.
  • To understand how droplet formation influences the structural behavior of PR repeats.
  • To explore the role of concentrated environments in protein folding and aggregation.

Main Methods:

  • Fourier transform infrared (FTIR) spectroscopy.
  • Two-dimensional infrared (2DIR) spectroscopy.
  • Analysis of amide-I band spectra to determine secondary structure.

Main Results:

  • Formation of PR20 droplets was observed.
  • Amide-I spectra showed changes consistent with secondary structure formation.
  • Spectroscopic data indicated folding into poly-proline helical structures within droplets.

Conclusions:

  • LLPS of PR dipeptide repeats induces secondary structure formation.
  • Concentration and crowding within droplets promote poly-proline helix formation.
  • This structural change may be a key step in the nucleation of pathogenic protein aggregates.