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Related Concept Videos

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...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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...
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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

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Related Experiment Video

Updated: Jun 25, 2026

Molecular Entanglement and Electrospinnability of Biopolymers
07:59

Molecular Entanglement and Electrospinnability of Biopolymers

Published on: September 3, 2014

Dyestuff-fibre interactions.

D M Lewis1

  • 1Department of Colour Chemistry & Dyeing, University of Leeds, Leeds LS2 9JT, UK.

International Journal of Cosmetic Science
|February 28, 2009
PubMed
Summary
This summary is machine-generated.

Dye-fibre interactions are mostly non-covalent, except for reactive dyes. Research explores new methods for disperse dyeing hydrophilic fibres, improving textile sustainability and performance.

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Molecular Entanglement and Electrospinnability of Biopolymers
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10:44

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Area of Science:

  • Textile Chemistry
  • Materials Science
  • Dyeing Technology

Background:

  • Dye-fibre interactions dictate textile coloration and fastness properties.
  • Non-covalent interactions (van der Waals, electrostatic, etc.) are common for acid, cationic, disperse, and direct dyes.
  • Reactive dyes form covalent bonds, offering excellent wet fastness but posing environmental concerns due to salt usage and unfixed dye.

Purpose of the Study:

  • To investigate alternative dyeing strategies for improved sustainability and performance.
  • To explore methods for making hydrophilic fibres amenable to disperse dyeing.
  • To understand the role of solvophobic and other interactions in novel dyeing systems.

Main Methods:

  • Analysis of non-covalent dye-fibre interactions across various dye and fibre classes.
  • Evaluation of reactive dyeing limitations and proposed modifications for environmental improvement.
  • Development and testing of treatments to enable disperse dyeing of hydrophilic fibres like cotton, silk, and wool.

Main Results:

  • Non-covalent interactions are prevalent, with reactive dyes forming covalent bonds.
  • Reactive dyes face environmental challenges related to salt consumption and dye fixation.
  • Promising experimental treatments are being developed to adapt hydrophilic fibres for disperse dye application.

Conclusions:

  • Modifying cellulose or dye systems can mitigate environmental issues with reactive dyes.
  • Adapting hydrophilic fibres for disperse dyeing offers a valuable alternative for hydrophobic dye classes.
  • Further research into solvophobic and other interactions is crucial for advancing textile dyeing technologies.