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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.8K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.8K
Protein Organization01:24

Protein Organization

6.5K
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....
6.5K
Protein and Protein Structure02:15

Protein and Protein Structure

79.6K
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...
79.6K
Protein Folding01:22

Protein Folding

118.2K
Overview
118.2K
Amyloid Fibrils03:03

Amyloid Fibrils

9.5K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.5K
Conserved Binding Sites01:49

Conserved Binding Sites

4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Soaking Up Success: Sponge-Assisted Nanoparticle Transfection.

Research square·2026
Same author

Genetically Encoded Sterol-Modification of a Synthetic Intrinsically Disordered Protein Drives Its Self-Assembly Into Diverse Morphologies.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

All-PEG-Like Block Copolymers Self-Assemble into Stealth Nanocarriers for Drug Delivery.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Intrinsically Disordered Protein Coating for Oral Delivery of Peptide Drugs.

bioRxiv : the preprint server for biology·2025
Same author

Rational Design of Thermoresponsive Elastin-Like Protein Monolayers for Nonenzymatic Cell Harvesting.

Biomacromolecules·2025
Same author

Controlling Release Kinetics of an Adjuvant from a Depot Improves the Efficacy of Local Immunotherapy in Metastatic Cancer.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025
Same journal

Innate Immunity of Framework Nucleic Acids.

Accounts of chemical research·2026
Same journal

High-Performance CH-Series Non-Fullerene Acceptors for Organic Photovoltaics.

Accounts of chemical research·2026
Same journal

Design Principles for Negative Thermal Expansion in Two-Dimensional Materials.

Accounts of chemical research·2026
Same journal

Main Group Redox Catalysis: New Frontiers with Germanium and Tin.

Accounts of chemical research·2026
Same journal

Taming Irreversibility in sp<sup>2</sup>-Carbon-Conjugated COFs from Polycrystalline Powders to Single Crystals and Thin Films.

Accounts of chemical research·2026
Same journal

Electroactive Imidazolium Ionic Liquids in Organic Synthesis.

Accounts of chemical research·2026
See all related articles

Related Experiment Video

Updated: Jul 6, 2025

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

1.9K

Encoding Structure in Intrinsically Disordered Protein Biomaterials.

Rachel L Strader1, Yulia Shmidov1, Ashutosh Chilkoti1

  • 1Department of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.

Accounts of Chemical Research
|January 9, 2024
PubMed
Summary
This summary is machine-generated.

Synthetic intrinsically disordered proteins (SynIDPs) are engineered using nature-inspired strategies to create diverse structures and properties. These biomaterials offer tunable physiochemical characteristics for advanced applications.

More Related Videos

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

12.9K
Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.0K

Related Experiment Videos

Last Updated: Jul 6, 2025

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

1.9K
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

12.9K
Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.0K

Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Polymer Chemistry

Background:

  • Intrinsically disordered proteins (IDPs) lack stable 3D structures, unlike ordered proteins.
  • IDPs feature intrinsically disordered regions (IDRs) rich in specific amino acids.
  • Protein structure diversity is achieved in nature via hybridization and cross-linking.

Purpose of the Study:

  • To describe synthetic IDP (SynIDP)-based biomaterials developed over the past decade.
  • To highlight bioinspired strategies for introducing structural diversity into SynIDPs.
  • To emphasize the physiochemical properties and structural features of these engineered materials.

Main Methods:

  • Incorporating ordered domains into SynIDPs.
  • Conjugating SynIDPs to other moieties via genetic or chemical modification.
  • Engineering SynIDP topology through chemical modification.

Main Results:

  • Developed SynIDP-based biomaterials with tunable structures and properties.
  • Achieved structural diversity by combining different engineering approaches.
  • Created materials spanning nano- to macro-length scales.

Conclusions:

  • SynIDP engineering enables the creation of biomaterials with a wide range of structural possibilities.
  • These materials offer unique physiochemical properties inspired by nature.
  • Future directions focus on designing functional SynIDP-based biomaterials for biomedical applications.