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Related Concept Videos

Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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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...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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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...
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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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...
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Structural Protein Function01:56

Structural Protein Function

29.0K
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...
29.0K
Fibrous Proteins00:55

Fibrous Proteins

3.7K
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...
3.7K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Related Experiment Video

Updated: Oct 21, 2025

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

Published on: September 20, 2012

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Structure of Collagen.

Chenxi Zhao1, Yuelong Xiao2, Shengjie Ling1

  • 1School of Physical Science and Technology, ShanghaiTech University, Shanghai, China.

Methods in Molecular Biology (Clifton, N.J.)
|September 2, 2021
PubMed
Summary
This summary is machine-generated.

Collagen, the most abundant fibrous protein, provides structural support and regulates cell functions. Understanding its hierarchical structure, from primary to quaternary levels, is key for tissue engineering and biomaterials.

Keywords:
CollagenHierarchical structureα-helix

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Area of Science:

  • Biochemistry
  • Materials Science
  • Cell Biology

Background:

  • Collagen is the most abundant fibrous protein, crucial for mechanical support and cellular processes like adhesion and repair.
  • It is a primary component in connective tissues, including skin, bone, and cartilage.
  • Understanding collagen's structure is vital for its applications in biomaterials and tissue engineering.

Purpose of the Study:

  • To systematically introduce the hierarchical structure of collagen.
  • To provide theoretical guidance for the application of collagen-based materials.
  • To focus on the structure of type I collagen due to its prevalence.

Main Methods:

  • Review of collagen's hierarchical structure.
  • Detailed examination from primary to quaternary structural levels.
  • Focus on type I collagen structure.

Main Results:

  • Collagen exhibits a hierarchical structure spanning from primary to quaternary levels.
  • Type I collagen's specific structural features are highlighted.
  • The structure-function relationship of collagen is elucidated.

Conclusions:

  • A comprehensive understanding of collagen's hierarchical structure is essential.
  • This knowledge supports the development and application of collagen scaffolds.
  • Focusing on type I collagen provides foundational insights into collagen biology and biomaterials.