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Related Concept Videos

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...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

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Related Experiment Video

Updated: Jun 21, 2026

Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction
10:37

Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction

Published on: January 16, 2014

Fibulin 5 forms a compact dimer in physiological solutions.

Richard P O Jones1, Ming-Chuan Wang, Thomas A Jowitt

  • 1Genetic Medicine, Manchester Academic Health Science Centre, Faculty of Medical and Human Sciences, University of Manchester, Manchester M13 9PL, United Kingdom.

The Journal of Biological Chemistry
|July 21, 2009
PubMed
Summary
This summary is machine-generated.

Fibulin 5, crucial for elastic tissue formation, forms dimers under physiological conditions. This dimerization, driven by calcium-binding epidermal growth factor domains, may regulate its function in elastinogenesis.

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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Extracellular Matrix Biology

Background:

  • Fibulin 5 is an extracellular matrix protein vital for elastic tissue development.
  • Mutations in fibulin 5 are linked to cutis laxa and age-related macular degeneration.

Purpose of the Study:

  • To elucidate the structure, hydrodynamics, and oligomerization state of fibulin 5.
  • To understand the mechanism and physiological relevance of fibulin 5 dimerization.

Main Methods:

  • Small angle X-ray scattering (SAXS)
  • Electron microscopy (EM)
  • Light scattering
  • Circular dichroism
  • Sedimentation analysis

Main Results:

  • SAXS and EM revealed compact monomer structures for fibulin 5.
  • EM demonstrated monomer association into dimers around a central cavity.
  • Dimerization equilibrium is influenced by NaCl and Ca2+ concentrations, favoring dimers under physiological conditions.
  • Dimerization is mediated by calcium-binding epidermal growth factor (cbEGF) domains.

Conclusions:

  • Fibulin 5 exists predominantly as a dimer under physiological conditions.
  • Dimerization, driven by cbEGF domains, may be critical for fibulin 5's role in elastinogenesis.
  • Dimer formation could regulate interactions with binding partners like tropoelastin.