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

Fibril-associated Collagen01:11

Fibril-associated Collagen

2.6K
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
2.6K
Structural Protein Function01:56

Structural Protein Function

27.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
27.9K
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

2.3K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
2.3K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

4.3K
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
4.3K
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

2.7K
In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
2.7K
Extracellular Matrix01:26

Extracellular Matrix

3.1K
Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
3.1K

You might also read

Related Articles

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

Sort by
Same author

Local deformation and dynamics of cross-linked hyaluronic acid gels at charged interfaces.

Soft matter·2025
Same author

Nanoparticle Dynamics near Polyacrylamide Gel Interfaces.

ACS polymers Au·2025
Same author

Effect of polyacrylamide gel elasticity on collagen type II fibril assembly.

Soft matter·2024
Same author

Optimizing anisotropic transport on bioinspired sawtooth surfaces.

Soft matter·2024
Same author

Effect of Polymer Gel Elasticity on Complex Coacervate Phase Behavior.

ACS polymers Au·2024
Same author

Effects of Molecular Weight and Surface Interactions on Polymer Diffusion in Confinement.

ACS macro letters·2023
Same journal

Metastable excited states of iodide-alkyl halide cluster anions: Insights from photodetachment spectroscopy and non-Hermitian quantum chemistry.

The Journal of chemical physics·2026
Same journal

Pressure-induced thermal expansion anomalies in dhcp iron hydride associated with magnetoelastic coupling.

The Journal of chemical physics·2026
Same journal

Seniority eigenstate configuration interaction.

The Journal of chemical physics·2026
Same journal

A data-driven modeling study on the accurate identification of Doppler-free saturated absorption spectra in diatomic tellurium (130Te2).

The Journal of chemical physics·2026
Same journal

Anharmonic phonons via quantum thermal bath simulations.

The Journal of chemical physics·2026
Same journal

Quantum simulation of alignment dependent differential cross sections in co-propagating molecular beams at cold collision energies.

The Journal of chemical physics·2026
See all related articles

Related Experiment Video

Updated: Aug 12, 2025

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

17.1K

Ionic environment effects on collagen type II persistence length and assembly.

Kathryn G Wilcox1, Grace M Kemerer1, Svetlana Morozova1

  • 1Department of Macromolecular Science and Engineering, Case Western Reserve University, Cleveland, Ohio 44106, USA.

The Journal of Chemical Physics
|February 1, 2023
PubMed
Summary
This summary is machine-generated.

Collagen

More Related Videos

Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

497
Layer-by-layer Collagen Deposition in Microfluidic Devices for Microtissue Stabilization
09:56

Layer-by-layer Collagen Deposition in Microfluidic Devices for Microtissue Stabilization

Published on: September 29, 2015

9.5K

Related Experiment Videos

Last Updated: Aug 12, 2025

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

17.1K
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

497
Layer-by-layer Collagen Deposition in Microfluidic Devices for Microtissue Stabilization
09:56

Layer-by-layer Collagen Deposition in Microfluidic Devices for Microtissue Stabilization

Published on: September 29, 2015

9.5K

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Collagen type II is crucial for cartilage structure and fibril formation.
  • Fibril size is theorized to be limited by electrostatics and collagen elasticity.
  • Persistence length (lp) quantifies collagen's elasticity.

Purpose of the Study:

  • Investigate collagen triple helix structure and fibril size scales under varying ionic conditions.
  • Determine the impact of pH and salt concentration on collagen's physical properties.
  • Relate collagen persistence length to fibril assembly mechanisms.

Main Methods:

  • Static and dynamic light scattering to measure collagen triple helix properties (Rg, Rh, A2).
  • Calculation of persistence length (lp) from experimental data.
  • Electron microscopy to determine fibril diameter in specific conditions.

Main Results:

  • Collagen triple helix lp varied with ionic strength, decreasing at pH 2 and increasing at pH 7.4.
  • Intrinsic lp of collagen triple helix was determined to be 90-95 nm at zero net backbone interaction.
  • Fibril diameter was measured and compared with lp using theoretical models.

Conclusions:

  • Ionic environment significantly influences collagen triple helix elasticity and fibril assembly.
  • Understanding collagen lp is key to elucidating biomacromolecule self-assembly processes.
  • This study provides insights into collagen's role in cartilage structure and disease.