Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Protein and Protein Structure

Protein and Protein Structure

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...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

What are Proteins?

What are Proteins?

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

You might also read

Related Articles

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

Sort by

Same author

Structural and Functional Elements of the Epidermal Appendages in Birds and Reptiles: Conformations and Modes of Assembly of the Constituent β-Filaments and Keratin Intermediate Filaments (IF).

Sub-cellular biochemistry·2026

Same author

Comparative Study of the Positions of Glycosylated Residues in the Chains of Fibril-Forming Collagens and the Role that These Residues Play in Axial and Lateral Assembly.

Sub-cellular biochemistry·2026

Same author

John Squire: a leader and seminal contributor to experimental and theoretical muscle research for over 50 years.

Journal of muscle research and cell motility·2023

Same author

Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.

The Journal of cell biology·2023

Same author

Potential implications of the glycosylation patterns in collagen α1(I) and α2(I) chains for fibril assembly and growth.

Journal of structural biology·2023

Same author

An experimental model of contusion injury in humans.

PloS one·2022

Search research articles

Related Experiment Video

Updated: Feb 10, 2026

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics

Published on: November 27, 2017

Trichocyte Keratin-Associated Proteins (KAPs).

R D Bruce Fraser^1,2, David A D Parry^3,4

¹Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand.

Advances in Experimental Medicine and Biology

|May 26, 2018

Summary

This summary is machine-generated.

Keratin-associated proteins (KAPs) are crucial for hair fiber structure and durability. Their three-dimensional structures and roles in hair diseases are complex, involving gene expression modulation rather than mutations.

Keywords:

Filament-matrix composite High-glycine-tyrosine proteins High-sulfur proteins Matrix-related hair diseases Paracortex and orthocortex Physical attributes of trichocyte keratin Sequence repeats in matrix proteins Ultra-high-sulfur proteins

More Related Videos

Synthesis of Keratin-based Nanofiber for Biomedical Engineering

Synthesis of Keratin-based Nanofiber for Biomedical Engineering

Published on: February 7, 2016

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Published on: January 6, 2015

Related Experiment Videos

Last Updated: Feb 10, 2026

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics

Published on: November 27, 2017

Synthesis of Keratin-based Nanofiber for Biomedical Engineering

Synthesis of Keratin-based Nanofiber for Biomedical Engineering

Published on: February 7, 2016

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Published on: January 6, 2015

Area of Science:

Biochemistry
Structural Biology
Dermatology

Background:

Trichocytes form epidermal appendages like hair, featuring a filament-matrix composite structure.
Human hair keratin intermediate filaments (IF) are embedded in a matrix of at least 89 keratin-associated proteins (KAPs).
KAPs are classified into three families based on cysteine or glycine-tyrosine content.

Purpose of the Study:

To explore the structural characteristics of keratin-associated proteins (KAPs).
To understand the role of KAPs in hair fiber organization and physical properties.
To investigate the involvement of KAPs in hair diseases.

Main Methods:

Analysis of available KAP sequence data.
Bioinformatic modeling to predict three-dimensional structures.
Review of current literature on KAP function and disease association.

Main Results:

KAPs organize IF into macrofibrils, influencing hair hardness, toughness, and pliability.
KAPs enhance hair durability and resistance to microbial degradation.
KAP conformations in vivo are likely diverse, stabilized by disulfide bonds.

Conclusions:

KAPs play a vital role in determining the physical properties and structural integrity of hair fibers.
Understanding KAP structure-function relationships is key to comprehending hair biology.
The role of KAPs in hair diseases is primarily linked to gene expression modulation.