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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...
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...
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...
Phases of Wound Repair01:28

Phases of Wound Repair

Following injury, the integrity of the injured tissues must be reestablished. For example, in skin tissue, wound repair involves coordination among resident skin cells, blood mononuclear cells, extracellular matrix, growth factors, and cytokines to complete the healing cascade.
Formation of Blood Clot
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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...

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Related Experiment Video

Updated: Jun 23, 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

High pressure stabilization of collagen structure.

S A Potekhin1, A A Senin, N N Abdurakhmanov

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. spot@vega.protres.ru

Biochimica Et Biophysica Acta
|April 21, 2009
PubMed
Summary

High pressure enhances collagen stability, increasing denaturation temperature. Collagen denaturation volume changes are significant and pressure-dependent, unlike most globular proteins.

More Related Videos

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

Related Experiment Videos

Last Updated: Jun 23, 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

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

Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Collagen is a crucial structural protein.
  • Understanding collagen's response to pressure is vital for various applications.
  • High-pressure studies reveal insights into protein stability and denaturation.

Purpose of the Study:

  • To investigate the heat denaturation of collagen under high pressure.
  • To quantify the effect of pressure on collagen's structural stability and thermodynamic properties.
  • To compare collagen denaturation with that of globular proteins.

Main Methods:

  • Scanning microcalorimetry was employed to study heat denaturation.
  • Experiments were conducted at varying high-pressure conditions.
  • Thermodynamic parameters like enthalpy and cooperativity were analyzed.

Main Results:

  • A pressure increase of 200 MPa raised collagen stability by 6.8°C.
  • Pressure did not significantly alter transition cooperativity but slightly decreased enthalpy.
  • Collagen denaturation involves a significant partial specific volume increase, distinct from globular proteins.
  • The volume increment decreased with pressure due to compressibility differences, altering sign around 324 MPa.

Conclusions:

  • Collagen exhibits unique volume changes during denaturation compared to globular proteins.
  • High pressure enhances collagen stability up to a critical point (324 MPa).
  • Further pressure increases beyond this point lead to collagen destabilization.