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Related Concept Videos

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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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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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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Structural Protein Function01:56

Structural Protein Function

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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...
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Fibrous Proteins00:55

Fibrous Proteins

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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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Protein and Protein Structure02:15

Protein and Protein Structure

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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...
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Related Experiment Video

Updated: May 3, 2026

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

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Bacterial collagen-like proteins that form triple-helical structures.

Zhuoxin Yu1, Bo An2, John A M Ramshaw3

  • 1Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA.

Journal of Structural Biology
|January 18, 2014
PubMed
Summary

Bacterial collagens, identified through genome analysis, share animal collagen's triple-helix structure. These novel recombinant proteins offer a new platform for studying collagen and developing advanced biomedical materials.

Keywords:
Biomedical materialCollagenProkaryoteRecombinant expressionThermal stabilityTriple-helix

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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Production of Nanofibrillar Patterned Collagen for Tissue Engineering
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Last Updated: May 3, 2026

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomaterials Science

Background:

  • Collagen-like proteins have been identified in bacteria, sharing the Gly-Xaa-Yaa repeat characteristic of animal collagens.
  • These bacterial collagens adopt a triple-helix conformation but lack hydroxyproline, a stabilizing post-translational modification found in animal collagens.

Purpose of the Study:

  • To investigate the structural and functional properties of bacterial collagens.
  • To explore the potential of bacterial collagens as novel biomedical materials.

Main Methods:

  • Genome database analysis to identify bacterial collagen-like proteins.
  • Expression of bacterial collagens in Escherichia coli.
  • Analysis of triple-helix conformation and thermal stability.

Main Results:

  • Bacterial collagens adopt a triple-helix structure despite lacking hydroxyproline.
  • These proteins exhibit high thermal stability (35-39°C), comparable to mammalian collagens.
  • Bacterial collagens can be produced in large quantities using recombinant methods and are amenable to genetic modification.

Conclusions:

  • Bacterial collagens represent a new family of recombinant proteins with potential applications in research and biomaterials.
  • Their structural and functional motifs can be investigated, and they can be engineered for specific biomedical functions.