1932

Abstract

Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen—the prototypical collagen fibril—has been revealed in detail. Artificial collagen fibrils that display some properties of natural collagen fibrils are now accessible using chemical synthesis and self-assembly. A rapidly emerging understanding of the mechanical and structural properties of native collagen fibrils will guide further development of artificial collagenous materials for biomedicine and nanotechnology.

[Erratum, Closure]

An erratum has been published for this article:
Collagen Structure and Stability
Loading

Article metrics loading...

/content/journals/10.1146/annurev.biochem.77.032207.120833
2009-07-07
2024-03-28
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.biochem.77.032207.120833
Loading
/content/journals/10.1146/annurev.biochem.77.032207.120833
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error