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- W2086149600 endingPage "32" @default.
- W2086149600 startingPage "21" @default.
- W2086149600 abstract "Collagens contain large numbers of Gly-Xaa-Yaa peptide repeats that form the characteristic triple helix, where the individual chains fold into a polyproline II helix and three of these helices form a right-handed triple helix. For the proper folding of the triple helix collagens contain trimerization domains. These domains ensure a single starting point for triple helix formation and are also responsible for the chain selection in heterotrimeric collagens. Trimerization domains are non-collagenous domains of very different structures. The size of trimerization domains varies from 35 residues in type IX collagen to around 250 residues for the fibrillar collagens. These domains are not only crucial for biological functions, but they are also attractive tools for generating recombinant collagen fragments of interest as well as for general use in protein engineering and biomaterial design. Here we review the current knowledge of the structure and function of these trimerization domains." @default.
- W2086149600 created "2016-06-24" @default.
- W2086149600 creator A5012954903 @default.
- W2086149600 creator A5063332506 @default.
- W2086149600 creator A5091312244 @default.
- W2086149600 date "2012-01-01" @default.
- W2086149600 modified "2023-10-06" @default.
- W2086149600 title "The crucial role of trimerization domains in collagen folding" @default.
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