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

Structural Protein Function01:56

Structural Protein Function

30.3K
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...
30.3K
Fibril-associated Collagen01:11

Fibril-associated Collagen

3.5K
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...
3.5K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

6.1K
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...
6.1K
Radical Chain-Growth Polymerization: Chain Branching01:17

Radical Chain-Growth Polymerization: Chain Branching

2.6K
The skeletal structure of polymers synthesized via radical polymerization is always branched. For example, the polymerization of ethylene by radical polymerization results in a low-density grade of polyethylene with a heavily branched skeletal structure. Here, the radical site abstracts hydrogen from the growing chain, and the radical site shifts from the end (a primary carbon center) to anywhere within the growing chain (a secondary carbon center). Consequently, the part of the chain from the...
2.6K
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

3.2K
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...
3.2K
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

You might also read

Related Articles

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

Sort by
Same author

Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network.

The Journal of biological chemistry·2026
Same author

Collagen IV of basement membrane: V. Bromide-mediated sulfilimine bonds interlock the quaternary structure of NC1-hexamer of scaffolds enabling metazoan evolution.

The Journal of biological chemistry·2026
Same author

Collagen IV of basement membrane: V. Bromide-mediated sulfilimine bonds interlock the quaternary structure of NC1-hexamer of scaffolds enabling metazoan evolution.

bioRxiv : the preprint server for biology·2026
Same author

Fibulin-4 is required for the mechanical stability of tendons.

Cell and tissue research·2025
Same author

Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.

Matrix biology : journal of the International Society for Matrix Biology·2025
Same author

Targeted incorporation of collagen IV to the basement membrane: A step forward for developing extracellular protein therapies.

The Journal of biological chemistry·2025

Related Experiment Video

Updated: Mar 11, 2026

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

17.9K

Structural insight for chain selection and stagger control in collagen.

Sergei P Boudko1,2,3, Hans Peter Bächinger1,2

  • 1Research Department, Shriners Hospital for Children, Portland, Oregon 97239, USA.

Scientific Reports
|November 30, 2016
PubMed
Summary

Researchers discovered how collagen chains assemble, revealing the structural basis for chain selection and stagger formation in collagen molecules. This finding aids in generating specific collagen fragments with native composition and stagger.

More Related Videos

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
07:12

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

2.9K
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

1.0K

Related Experiment Videos

Last Updated: Mar 11, 2026

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

17.9K
Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
07:12

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

2.9K
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

1.0K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Collagen is essential for metazoans, forming a triple helix with specific glycine placement.
  • Collagen molecules can be homo- or hetero-trimeric, composed of one to three distinct polypeptide chains.
  • Mechanisms controlling collagen chain composition and stagger during folding are not fully understood.

Purpose of the Study:

  • To elucidate the structural basis for chain selection in collagen assembly.
  • To understand the mechanisms governing stagger formation in collagen molecules.
  • To explore the potential for generating native collagen fragments.

Main Methods:

  • Analysis of the non-collagenous domain 2 (NC2) of type IX collagen.
  • Investigating the assembly of three distinct chains (α1, α2, α3) within NC2.
  • Structural elucidation of chain guidance and stagger formation.

Main Results:

  • The NC2 domain of type IX collagen dictates chain selection and stagger formation.
  • Specific chain positions (leading, middle, trailing) are guided by the assembled α1, α2, and α3 chains.
  • A structural basis for controlling collagen composition and stagger has been uncovered.

Conclusions:

  • The NC2 domain acts as a molecular template for collagen assembly.
  • Understanding this mechanism allows for precise control over collagen structure.
  • This research facilitates the generation of collagen fragments with native properties.