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Collagen Structure and Stability

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TLDR
The fibrillar structure of type I collagen-the prototypical collagen fibril-has been revealed in detail and will guide further development of artificial collagenous materials for biomedicine and nanotechnology.
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.

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References
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Journal ArticleDOI

Protein folding and misfolding

TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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Mechanics of Motor Proteins and the Cytoskeleton

TL;DR: The Motility Models: From Crossbridges to Motion chapter describes the building blocks of the Cytoskeleton and some of the mechanisms used in its manufacture are described.
Journal ArticleDOI

Structure of the cross-beta spine of amyloid-like fibrils.

TL;DR: The atomic structure of the cross-β spine illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.
Journal ArticleDOI

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

TL;DR: The proteasome contains deubiquitinating enzymes (DUBs) that can remove ubiquitin before substrate degradation initiates, thus allowing some substrates to dissociate from the proteasomes and escape degradation.
Journal ArticleDOI

Collagen fibril formation

TL;DR: Preliminary evidence from invertebrates is included which suggests that the principles for bipolar fibril assembly were established at least 500 million years ago, and how mature fibrils are assembled from early fibrILS is reviewed.
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