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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 form...

Fibril-associated Collagen

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...

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Related Experiment Video

Updated: Jun 19, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Published on: July 25, 2012

Peptidic "Molecular Beacon" for Collagen.

Jinyi Yang¹, Yifan Quan^1,2, Yifu Ouyang^1,2

¹Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.

Biomacromolecules

|September 3, 2024

Summary

This summary is machine-generated.

Researchers developed a new ratiometric molecular beacon for detecting damaged collagen. This peptide-based probe offers a novel method for identifying collagen abnormalities in biological settings.

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Published on: January 31, 2014

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Last Updated: Jun 19, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

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Published on: July 25, 2012

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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Published on: September 20, 2012

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Area of Science:

Biochemistry
Biophysics
Materials Science

Background:

Collagen-mimetic peptides (CMPs) are crucial for studying collagen structure and function.
Current CMP probes for damaged collagen lack ratiometric detection capabilities.

Purpose of the Study:

To develop a ratiometric molecular beacon for detecting damaged collagen.
To guide the design of CMP-based probes by determining end-to-end distances.

Main Methods:

Electron Paramagnetic Resonance (EPR) spectroscopy was used to measure end-to-end distances of CMPs.
A specific tripeptide repeat sequence with a fluorophore-quencher pair (EDANS-DABCYL) was synthesized.

Main Results:

End-to-end distances of non-helical CMPs were shorter than those in collagen triple helices.
The developed molecular beacon enabled ratiometric detection of binding to other CMPs and natural collagen.

Conclusions:

Shorter end-to-end distances in non-helical CMPs suggest their utility as molecular beacons.
This study provides a foundation for a new ratiometric detection modality for damaged collagen in vivo.