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Related Concept Videos

Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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...
Structural Protein Function01:56

Structural Protein Function

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 form...
Structural Protein Function01:56

Structural Protein Function

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 form...
Fibril-associated Collagen01:11

Fibril-associated Collagen

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...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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 exist in...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...

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Related Experiment Video

Updated: Jun 24, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Collagen structure and stability.

Matthew D Shoulders1, Ronald T Raines

  • 1Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA.

Annual Review of Biochemistry
|April 7, 2009
PubMed
Summary
This summary is machine-generated.

Collagen, the most abundant animal protein, forms stable triple helices due to stereoelectronic effects. Advances in understanding collagen structure and artificial fibril synthesis pave the way for new biomaterials.

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

Related Experiment Videos

Last Updated: Jun 24, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

Area of Science:

  • Biochemistry
  • Biomaterials Science
  • Structural Biology

Background:

  • Collagen is the most abundant structural protein in animals.
  • Its triple helix structure is crucial for stability and function.
  • Understanding collagen is key for developing advanced biomaterials.

Purpose of the Study:

  • To elucidate the structure and stability of collagen triple helices.
  • To detail the fibrillar structure of type I collagen.
  • To explore the development of artificial collagen fibrils.

Main Methods:

  • Analysis of collagen triple helix structure and stability.
  • Detailed structural elucidation of type I collagen fibrils.
  • Chemical synthesis and self-assembly techniques for artificial collagen fibrils.

Main Results:

  • Stereoelectronic effects and preorganization are key to collagen stability.
  • The fibrillar structure of type I collagen has been revealed.
  • Artificial collagen fibrils with natural properties are now achievable.

Conclusions:

  • New insights into collagen stability mechanisms have been established.
  • Artificial collagen fibrils can be synthesized, mimicking natural properties.
  • Understanding collagen mechanics and structure will drive innovation in biomedicine and nanotechnology.