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.
Keywords
Polyproline helixFibrilCollagen fibrilChemistryTriple helixBiophysicsType I collagenCollagen helixStructural stabilityPeptideBiochemistryStereochemistryBiology
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Publication Info
- Year
- 2009
- Type
- review
- Volume
- 78
- Issue
- 1
- Pages
- 929-958
- Citations
- 3542
- Access
- Closed
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Cite This
Matthew D. Shoulders,
Ronald T. Raines
(2009).
Collagen Structure and Stability.
Annual Review of Biochemistry
, 78
(1)
, 929-958.
https://doi.org/10.1146/annurev.biochem.77.032207.120833
Identifiers
- DOI
- 10.1146/annurev.biochem.77.032207.120833