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

Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

45.5K
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...
45.5K
Fibrous Proteins00:55

Fibrous Proteins

3.7K
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...
3.7K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

23.2K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
23.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.2K
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...
3.2K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

3.3K
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...
3.3K
Globular Proteins01:27

Globular Proteins

9.1K
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
9.1K

You might also read

Related Articles

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

Sort by
Same author

Intraoperative Hemorrhage during Implantable Collamer Lens Surgery: A Case Report and Management Strategy.

Case reports in ophthalmology·2025
Same author

A Generative Foundation Model for Scalable Cytology Image Synthesis in AI-Powered Diagnostics.

Clinical cancer research : an official journal of the American Association for Cancer Research·2025
Same author

A highly photostable monomeric red fluorescent protein for dual-color 3D STED and time-lapse 3D SIM imaging.

Nature methods·2025
Same author

miR-7213-5p-mediated suppression of CCL19 in fibroblast cells may attenuate lupus nephritis.

Clinical and experimental medicine·2025
Same author

The protective role of appendicular lean mass in osteoporosis development among postmenopausal type 2 diabetes patients.

Scientific reports·2025
Same author

Leucine Attenuates Osteoarthritis via mTORC1/LXRα-Mediated Macrophage Reprogramming and Rspo2/β-Catenin Axis Suppression.

Cartilage·2025

Related Experiment Video

Updated: Oct 21, 2025

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

12.7K

Gelation Methods to Assemble Fibrous Proteins.

Ning Fan1, Ke Zheng2

  • 1Biomass Molecular Engineering Center and Department of Materials Science and Engineering, School of Forestry and Landscape Architecture, Anhui Agricultural University, Hefei, Anhui, China.

Methods in Molecular Biology (Clifton, N.J.)
|September 2, 2021
PubMed
Summary

Fibrous protein hydrogels are made using physical or chemical gelation methods. These processes involve protein molecule aggregation into organized nanofibrillar networks, triggered by various factors or cross-linking reactions.

Keywords:
Chemical gelationFibrous proteinsPhysical gelation

More Related Videos

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

6.0K
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

14.0K

Related Experiment Videos

Last Updated: Oct 21, 2025

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

12.7K
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

6.0K
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

14.0K

Area of Science:

  • Biomaterials Science
  • Materials Chemistry
  • Protein Engineering

Background:

  • Gelation is a key process for fabricating fibrous protein materials.
  • Protein molecules aggregate from random structures into organized networks like nanofibrillar structures.
  • Fibrous protein gelation can be classified into physical and chemical methods based on their underlying mechanisms.

Purpose of the Study:

  • To summarize protocols for preparing fibrous protein hydrogels.
  • To highlight the mechanisms of physical and chemical gelation methods.
  • To provide a comprehensive overview of fibrous protein hydrogel fabrication.

Main Methods:

  • Physical gelation: conformational transformation of fibroin proteins triggered by temperature, concentration, pH, or shear force.
  • Chemical gelation: cross-linking of fibrous proteins via chemical and/or enzymatic reactions.
  • Review of established and emerging protocols for hydrogel preparation.

Main Results:

  • Detailed protocols for both physical and chemical gelation methods are presented.
  • Mechanisms driving each gelation type are elucidated.
  • The formation of organized nanofibrillar networks from protein aggregation is demonstrated.

Conclusions:

  • Gelation offers an efficient route to fabricate advanced fibrous protein materials.
  • Understanding the distinct mechanisms of physical and chemical gelation is crucial for material design.
  • This work provides essential protocols and mechanistic insights for fibrous protein hydrogel synthesis.