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Related Concept Videos

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...
Elastin is Responsible for Tissue Elasticity01:12

Elastin is Responsible for Tissue Elasticity

Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
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Extracellular Matrix01:26

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Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
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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Members Made of Elastoplastic Material

The behavior of elastoplastic materials under bending stresses, particularly in structural members with rectangular cross-sections, is crucial for predicting material responses and understanding failure modes. Initially, when a bending moment is applied, the stress distribution across the section follows Hooke's Law and is linear and elastic. This distribution means the stress increases from the neutral axis to the maximum at the outer fibers, up to the elastic limit.
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Non-contact, Label-free Monitoring of Cells and Extracellular Matrix using Raman Spectroscopy
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Molecular biophysics of elastin structure, function and pathology

D W Urry1, C H Luan, S Q Peng

  • 1Laboratory of Molecular Biophysics, School of Medicine, University of Alabama at Birmingham 35294-0019, USA.

Ciba Foundation Symposium
|January 1, 1995
PubMed
Summary
This summary is machine-generated.

Elastin's structure involves beta-turns and helical folding, driven by temperature-dependent hydrophobic interactions. This inverse temperature transition (Tt) scale reveals amino acid hydrophobicity, explaining elastin's role in various physiological and pathological processes.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Materials Science

Background:

  • Elastin's unique molecular structure, characterized by recurring hydrophobic sequences (XPGX'), dictates its elastic properties.
  • The self-assembly of elastin into filaments is primarily driven by hydrophobic interactions and inverse temperature transitions.

Purpose of the Study:

  • To develop a novel hydrophobicity scale for amino acids based on elastin's hydrophobic folding and assembly.
  • To elucidate the role of temperature-induced hydrophobic transitions in elastin's structure and function.
  • To explain the molecular mechanisms underlying elastogenesis, emphysema, solar elastosis, and scar tissue formation.

Main Methods:

  • Utilized synthetic polypeptides poly[fv(VPGVG),fx(VPGXG)] to study hydrophobic folding and assembly.
  • Determined the onset of inverse temperature transition (Tt) for various amino acid substitutions.
  • Correlated Tt values with amino acid hydrophobicity and elastin-related processes.

Main Results:

  • Established a new hydrophobicity scale based on Tt, with hydrophobic residues (Tyr, Phe) showing low Tt and hydrophilic residues (Glu, Asp, Lys) showing high Tt.
  • Demonstrated that altering Tt above or below physiological temperature controls elastin chain unfolding/assembly.
  • Showed that oxidation/photolysis irreversibly increases Tt, leading to elastin fiber damage.

Conclusions:

  • The delta Tt mechanism, based on temperature-induced hydrophobic transitions, is crucial for understanding elastin's structural dynamics.
  • This mechanism provides insights into the initiation of elastogenesis and the pathogenesis of diseases like pulmonary emphysema and solar elastosis.
  • Environmental factors like oxidation and UV exposure can irreversibly damage elastin by altering its hydrophobic properties.