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

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.9K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.7K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.7K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

4.0K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
4.0K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.7K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
3.7K
Protein and Protein Structure02:15

Protein and Protein Structure

89.6K
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...
89.6K
Fibrous Proteins00:55

Fibrous Proteins

4.8K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
4.8K

You might also read

Related Articles

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

Sort by
Same author

Introducing non-enzymatic crosslinks into atomistic simulations of collagen fibrils.

Bioinformatics (Oxford, England)·2026
Same author

SITH: A quantum-chemical framework for predicting bond destabilization in stretched molecules.

The Journal of chemical physics·2026
Same author

Directional dark field for nanoscale full-field transmission X-ray microscopy.

Light, science & applications·2026
Same author

KIMMDY: a biomolecular reaction emulator.

Nature communications·2026
Same author

Learning potential energy surfaces of hydrogen atom transfer reactions in peptides.

Digital discovery·2026
Same author

Precise Mechanochemical Scission of DNA Guided by Secondary Structures.

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: Feb 19, 2026

Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

27.5K

Stress-induced long-range ordering in spider silk.

Johannes A Wagner1,2, Sandeep P Patil3, Imke Greving4

  • 1Heidelberg Institute for Theoretical Studies (HITS), Heidelberg, 69118, Germany.

Scientific Reports
|November 12, 2017
PubMed
Summary

Mechanical load can induce long-range order in randomly arranged materials. This stress-induced ordering, observed in spider silk, arises from non-affine deformation enhancing density fluctuations.

More Related Videos

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure
10:26

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

5.8K
Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers
08:28

Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers

Published on: September 4, 2017

10.5K

Related Experiment Videos

Last Updated: Feb 19, 2026

Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

27.5K
Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure
10:26

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

5.8K
Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers
08:28

Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers

Published on: September 4, 2017

10.5K

Area of Science:

  • Materials Science
  • Mechanics of Materials
  • Biomaterials

Background:

  • The emergence of order from disordered states is a fundamental scientific question.
  • Understanding how mechanical forces influence material structure is crucial for developing advanced materials.

Purpose of the Study:

  • To investigate the emergence of long-range order in a randomly arranged two-phase material under mechanical load.
  • To demonstrate stress-induced ordering in spider dragline silk using experimental and computational methods.

Main Methods:

  • Small-Angle Neutron Scattering (SANS) experiments to probe mesoscopic structure.
  • Molecular Dynamics based finite element (FE) models to simulate material behavior.
  • Quantitative comparison of experimental and simulation results.

Main Results:

  • Evidence of stress-induced ordering in spider dragline silk under stretching.
  • Striking quantitative agreement between SANS and FE models regarding structural changes.
  • Demonstration that ordering is a general phenomenon arising from non-affine deformation, not material-specific processes.

Conclusions:

  • Mesoscopic long-range order can arise from disordered materials subjected to mechanical stress.
  • Non-affine deformation enhances density fluctuations, driving ordering.
  • This phenomenon is a general principle applicable to hybrid stiff-soft materials for property tuning.