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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...
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...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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...
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...
Fibrous Proteins00:55

Fibrous Proteins

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...

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Related Experiment Video

Updated: Jun 20, 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

Collagens.

Marion K Gordon1, Rita A Hahn

  • 1Department of Pharmacology and Toxicology, Rutgers University, Piscataway, NJ, USA. magordon@eohsi.rutgers.edu

Cell and Tissue Research
|August 21, 2009
PubMed
Summary
This summary is machine-generated.

Collagens are crucial extracellular matrix proteins providing structural integrity. This review details the structural characteristics of collagen types I-XXVIII, essential for tissue function.

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

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Published on: September 20, 2012

Generation of 3-D Collagen-based Hydrogels to Analyze Axonal Growth and Behavior During Nervous System Development
09:10

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Published on: June 25, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Collagens are a family of extracellular matrix proteins vital for cellular structural integrity and function.
  • They consist of three alpha chains forming a triple helix, characterized by repeating Glycine-X-Y peptide triplets.
  • Non-collagenous domains flank the triple helical regions, containing modules found in other matrix molecules.

Purpose of the Study:

  • To review the structural characteristics of collagen types I-XXVIII.
  • To highlight the importance of correctly assembled collagenous and non-collagenous domains for tissue function.

Main Methods:

  • Literature review of collagen structures.
  • Analysis of collagenous (Col) and non-collagenous domains.
  • Examination of peptide triplet composition (Glycine-X-Y).

Main Results:

  • Detailed structural features of collagen types I-XXVIII are presented.
  • The Glycine-X-Y triplet, with frequent proline and hydroxyproline at X and Y positions, is a key structural motif.
  • Non-collagenous domains exhibit diverse peptide modules, contributing to molecular interactions.

Conclusions:

  • Understanding collagen structure is fundamental to comprehending extracellular matrix assembly and tissue integrity.
  • The diverse structural characteristics across collagen types I-XXVIII underscore their varied roles in biology.
  • Proper molecular assembly of collagens is critical for maintaining tissue homeostasis and function.