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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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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...
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...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...

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Related Experiment Video

Updated: May 27, 2026

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens
06:08

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens

Published on: June 9, 2023

Fibrillar structures in food.

Ardy Kroes-Nijboer1, Paul Venema, Erik van der Linden

  • 1Physics & Physical Chemistry of Foods, Bomenweg 2, Wageningen, The Netherlands. ardy.nijboer@wur.nl

Food & Function
|November 19, 2011
PubMed
Summary
This summary is machine-generated.

Researchers explored the formation and properties of beta-lactoglobulin (β-lg) fibrils for use as functional food ingredients. Understanding fibril behavior in complex food systems is key for successful applications.

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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

Published on: September 20, 2012

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Last Updated: May 27, 2026

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens
06:08

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens

Published on: June 9, 2023

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:

  • Food science and technology
  • Biomaterials engineering
  • Protein chemistry

Background:

  • Protein and peptide fibril assembly is crucial in multiple scientific disciplines.
  • Protein fibrils are gaining attention as functional ingredients in the food industry.
  • Understanding fibril formation and characteristics is vital for their food applications.

Purpose of the Study:

  • To review recent research on beta-lactoglobulin (β-lg) fibril formation.
  • To elucidate the properties of β-lg fibrils.
  • To enhance control over the application of these fibrils in food products.

Main Methods:

  • Literature review of recent studies on β-lg fibrilization.
  • Analysis of the impact of research on the understanding of fibril formation processes.
  • Evaluation of the properties of formed β-lg fibrils.

Main Results:

  • Recent research has advanced the general understanding of β-lg fibril formation.
  • Properties of β-lg fibrils are better characterized, allowing for improved application control.
  • Identified a need for further research into fibril behavior within complex food matrices.

Conclusions:

  • Enhanced knowledge of β-lg fibril formation and properties facilitates better application strategies.
  • Further investigation is required to understand fibril interactions in complex food systems.
  • This research contributes to the development of novel functional food ingredients.