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Fibril-associated Collagen

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Related Experiment Video

Updated: May 24, 2026

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

Analysis of human collagen sequences.

Manisha Nassa¹, Pracheta Anand, Aditi Jain

¹Department of Biotechnology, Jaypee Institute of Information Technology, A-10, Sector-62, NOIDA, 201307, Uttar Pradesh, India.

|February 24, 2012

Summary

Collagen, a key extracellular matrix protein, has 28 human variants. This study analyzed alpha-1 collagen chains, identifying collagens 12, 14, and 20 as potential disease contributors due to unique structural properties.

Keywords:

Biocomputational tools Collagen Comparative characterization Extracellular matrix

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Last Updated: May 24, 2026

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

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Published on: January 31, 2014

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

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

Published on: September 20, 2012

Area of Science:

Biochemistry
Molecular Biology
Bioinformatics

Background:

The extracellular matrix (ECM) is crucial for cell interactions and support.
Collagen, the primary ECM component, is implicated in various diseases.
The large collagen family (28 human members) presents challenges in understanding individual structural functions.

Purpose of the Study:

To conduct a comparative analysis and characterization of human alpha-1 collagen sequences.
To utilize biocomputational tools for annotating collagen structures and functions.
To identify specific collagen types potentially involved in pathological conditions.

Main Methods:

Comparative analysis of human alpha-1 collagen sequences.
Physico-chemical characterization.
Secondary structural analysis.
Functional classification.
Phylogenetic analysis using biocomputational tools.

Main Results:

Identified collagens 12, 14, and 20 (FACIT family) as having atypical properties.
These collagens exhibit a high aliphatic index and low glycine/proline content.
Demonstrated evolutionary proximity among these specific collagen types.

Conclusions:

Collagens 12, 14, and 20 possess unique characteristics suggesting a role in disease.
These findings highlight potential candidates for further investigation in skeletal disorders.
Biocomputational analysis is valuable for understanding complex protein families like collagen.