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

138.7K
Overview
138.7K
Protein and Protein Structure02:15

Protein and Protein Structure

79.8K
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...
79.8K
Protein Folding01:22

Protein Folding

118.5K
Overview
118.5K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Peptide Bonds02:43

Peptide Bonds

74.9K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
74.9K
Termination of Translation01:44

Termination of Translation

25.5K
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...
25.5K

You might also read

Related Articles

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

Sort by
Same author

Photovoltaics for space applications.

Communications engineering·2026
Same author

Red Jujube Juice Fermented with <i>Pediococcus pentosaceus</i> and Its Antioxidant Activity in C2C12 Cells.

Foods (Basel, Switzerland)·2026
Same author

OrgLine: A versatile pipeline for organoid morphometry using detector-guided prompts.

Cell reports methods·2026
Same author

Effects of Polyethylene Microplastics on Seed Germination, Seedling Growth, and Physiological Characteristics of Maize.

Bulletin of environmental contamination and toxicology·2026
Same author

Cardiovascular-kidney-metabolic syndrome stages 0-3 and cognitive decline in Chinese adults: a longitudinal analysis from the China health and retirement longitudinal study.

BMC cardiovascular disorders·2026
Same author

Synergistic Strategies in the Design of Dynamic Hydrogels: Lessons From the Hydrogen Bonding in the Nature.

Macromolecular rapid communications·2026

Related Experiment Video

Updated: Jul 27, 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

13.0K

Secondary Structure-Governed Phase Separation Behavior in Glutamate-Based Polypeptides.

Mei Gao1, Yali Liu1, Chuanzhuang Zhao1

  • 1Faculty of Materials Science and Chemical Engineering, Ningbo University, Ningbo 315211, China.

Biomacromolecules
|June 9, 2023
PubMed
Summary
This summary is machine-generated.

Polypeptide secondary structures, like alpha-helices, critically influence biomacromolecule phase separation. Understanding this structure-property relationship aids in designing advanced peptide-based materials with tunable properties.

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
08:01

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

Published on: April 9, 2017

8.2K

Related Experiment Videos

Last Updated: Jul 27, 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

13.0K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
08:01

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

Published on: April 9, 2017

8.2K

Area of Science:

  • Biochemistry
  • Polymer Science
  • Materials Science

Background:

  • Biomacromolecule phase separation is vital in biological and medical applications.
  • Understanding the structural determinants of phase separation is crucial for designing functional peptide-based materials.

Purpose of the Study:

  • To investigate how primary and secondary structures of polypeptides regulate their phase separation behavior.
  • To establish a structure-property relationship for polypeptide phase separation.

Main Methods:

  • Synthesis of polypeptides with tunable hydroxyl-containing side chains.
  • Modulation of polypeptide secondary structure (e.g., helical content) via chemical environment and side chain composition.
  • Analysis of phase separation behavior, including cloud point temperature (Tcp) and hysteresis, during heating-cooling cycles.

Main Results:

  • Polypeptides with varying helical contents exhibited upper critical solution temperature behavior.
  • Phase transition temperature correlated with secondary structure content and interchain interactions.
  • The recovery rate of alpha-helical structure was found to govern the width of hysteresis during phase transitions.
  • Aggregation/deaggregation and secondary structure transitions were fully reversible.

Conclusions:

  • Polypeptide secondary structure content and dynamics directly impact phase separation behavior.
  • The study provides insights into controlling phase separation through secondary structure manipulation.
  • This work facilitates the rational design of peptide-based materials with predictable phase separation properties.