Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Fibrous Proteins00:55

Fibrous Proteins

4.8K
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...
4.8K
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

5.8K
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...
5.8K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

47.4K
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...
47.4K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

4.0K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
4.0K
Protein and Protein Structure02:15

Protein and Protein Structure

89.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
89.6K
Fibril-associated Collagen01:11

Fibril-associated Collagen

3.4K
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...
3.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Nonlinear relationships of fibrin network structure as a function of fibrinogen and thrombin concentrations for purified fibrinogen and plasma clots.

Acta biomaterialia·2026
Same author

The association between dietary macronutrient distribution and mortality in an African cohort.

The British journal of nutrition·2026
Same author

A randomized feasibility pilot trial of a remotely delivered physical activity intervention for adults with epilepsy.

Epilepsy & behavior : E&B·2026
Same author

Qualitative Study of Breast Cancer and Lymphoma Patients Participating in a Physical Activity Intervention: The Case for Tailored Physical Activity.

Cancer medicine·2026
Same author

A multi-layered approach to elucidate mechanisms of physical function in response to rehabilitation in heart failure with preserved ejection fraction.

medRxiv : the preprint server for health sciences·2026
Same author

Impact of Sedentary Time and Physical Function on Health-Related Quality of Life in Hospitalized Patients with Cardiovascular Disease.

CJC open·2025
Same journal

Evaluating a Novel Cell-Free Preservation Solution for Human Cardiomyocyte Protection: A Proof-of-Concept Study.

BioMed research international·2026
Same journal

Clinical Efficacy of Chinese Medicine in Treating Adult Henoch-Schönlein Purpura: A Meta-Analysis.

BioMed research international·2026
Same journal

RETRACTION: Rehabilitation Training and Resveratrol Improve the Recovery of Neurological and Motor Function in Rats after Cerebral Ischemic Injury through the Sirt1 Signaling Pathway.

BioMed research international·2026
Same journal

The Oncogenic and Tumor-Suppressive Roles of SNHG18: A Double-Edged Long Noncoding RNA in Cancer.

BioMed research international·2026
Same journal

Evaluation of LncRNA NEAT1 and MEG3 Expression Levels in Hospitalized COVID-19 Patients.

BioMed research international·2026
Same journal

Perceived Self-Efficacy and Its Determinants for Noncommunicable Disease Prevention Among Adults in Southern Ethiopia: A Community-Based Cross-Sectional Study.

BioMed research international·2026
See all related articles

Related Experiment Video

Updated: Feb 19, 2026

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
07:09

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States

Published on: April 1, 2015

12.0K

Nonuniform Internal Structure of Fibrin Fibers: Protein Density and Bond Density Strongly Decrease with Increasing

Wei Li1, Justin Sigley1, Stephen R Baker2

  • 1Department of Physics, Wake Forest University, Winston-Salem, NC 27109, USA.

Biomed Research International
|November 14, 2017
PubMed
Summary
This summary is machine-generated.

Fibrin fibers, crucial for blood clots, are not uniform. Thinner fibers are denser and stiffer, suggesting a dense core and sparse periphery, unlike control fibers.

More Related Videos

Controlled Strain of 3D Hydrogels under Live Microscopy Imaging
07:41

Controlled Strain of 3D Hydrogels under Live Microscopy Imaging

Published on: December 4, 2020

4.1K
Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

9.8K

Related Experiment Videos

Last Updated: Feb 19, 2026

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
07:09

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States

Published on: April 1, 2015

12.0K
Controlled Strain of 3D Hydrogels under Live Microscopy Imaging
07:41

Controlled Strain of 3D Hydrogels under Live Microscopy Imaging

Published on: December 4, 2020

4.1K
Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

9.8K

Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Fibrin fibers form the structural meshwork of blood clots.
  • Previous understanding assumed homogeneous internal structure and uniform protein/bond density in fibrin fibers, irrespective of diameter.

Purpose of the Study:

  • To investigate the internal structure and mechanical properties of fibrin fibers.
  • To determine how protein density and bond density vary with fibrin fiber diameter.

Main Methods:

  • Fibrin fibers were formed using fluorescently labeled fibrinogen.
  • Light intensity (I) and Young's modulus (Y) were measured as a function of fiber diameter (D).
  • Comparison with electrospun fibrinogen fibers as a control.

Main Results:

  • Fibrin fiber cross-sectional intensity scaled with D^1.4, indicating protein density decreases as D^-0.6.
  • Young's modulus scaled with D^-1.5, implying bond density also scales as D^-1.5.
  • Thinner fibrin fibers were denser and stiffer than thicker fibers.

Conclusions:

  • Fibrin fibers exhibit a heterogeneous internal structure with a dense core and a sparse periphery.
  • This non-uniformity contrasts with the homogeneous structure of control electrospun fibrinogen fibers.
  • Findings challenge the long-held assumption of homogeneous fibrin fiber structure.