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 Experiment Videos

Beta-silks: enhancing and controlling aggregation.

Cedric Dicko1, John M Kenney, Fritz Vollrath

  • 1Zoology Department, Oxford University, OX1 3PS, United Kingdom.

Advances in Protein Chemistry
|December 28, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Energy costs of Hannibal's alpine crossing.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Influence of PLDLA on the Rheological Properties of Regenerated Silk Fibroin-Based Gels.

Biomacromolecules·2026
Same author

pH-triggered clustering regulates β-sheet activation in silk assembly.

Communications chemistry·2026
Same author

Elephant habituation to drones as a behavioural observation tool.

Scientific reports·2025
Same author

Injectable bioresorbable conductive hydrogels for multimodal brain tumor electroimmunotherapy.

Nature communications·2025
Same author

Life History Plasticity and Gregarious Cocooning Behavior of the Wild Silkmoth <i>Cricula trifenestrata</i> Helfer (Lepidoptera: Saturniidae) on a Novel Host Plant, Cinnamon, in Thailand.

Insects·2025
Same journal

The plasma proteins and their fractionation.

Advances in protein chemistry·2010
Same journal

The preparation and criteria of purity of the amino acids.

Advances in protein chemistry·2010
Same journal

The use of protein and protein hydrolyzates for intravenous alimentation.

Advances in protein chemistry·2010
Same journal

The amino acid requirements of man.

Advances in protein chemistry·2010
Same journal

Reactions of native proteins with chemical reagents.

Advances in protein chemistry·2010
Same journal

The chemical determination of proteins.

Advances in protein chemistry·2010
See all related articles

Many proteins can form fibrils under specific conditions, not just specialized ones like silk. Protein environment significantly influences aggregation, similar to sequence, suggesting a universal mechanism for fiber formation.

Area of Science:

  • Biochemistry
  • Materials Science
  • Structural Biology

Background:

  • Fiber-forming proteins are not exclusive; many proteins can aggregate into fibrils under appropriate conditions.
  • Silk proteins serve as an ideal model for studying both forced and natural protein aggregation.
  • Proteins aggregate into ordered structures, with the surrounding environment playing a crucial role alongside the protein sequence.

Purpose of the Study:

  • To review the prerequisites for fiber formation in proteins.
  • To discuss the mechanisms animals use to facilitate and modulate silk assembly.
  • To explore controlled protein aggregation for diverse mechanical properties.

Main Methods:

  • Review of existing literature on protein aggregation and silk formation.

Related Experiment Videos

  • Analysis of the biological processes involved in silk production and fiber assembly.
  • Discussion of the interplay between protein sequence and environmental factors in aggregation.
  • Main Results:

    • A ubiquitous protein aggregation mechanism exists, influenced by both sequence and environment.
    • Silk proteins have evolved for efficient formation of insoluble, ordered structures.
    • Animals actively manage protein environments to control silk fiber assembly and properties.

    Conclusions:

    • Protein aggregation into fibers is a widespread phenomenon, not limited to specialized proteins.
    • The animal's control over the protein environment is key to achieving specific mechanical properties in silk.
    • Understanding these mechanisms can inform the design of novel biomaterials.