Fibrous long spacing type collagen fibrils have a hierarchical internal structure
- 11 April 2006
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 64 (1) , 227-233
- https://doi.org/10.1002/prot.20949
Abstract
Nanodissection of single fibrous long spacing (FLS) type collagen fibrils by atomic force microscopy (AFM) reveals hierarchical internal structure: Fibrillar subcomponents with diameters of ∼ 10 to 20 nm were observed to be running parallel to the long axis of the fibril in which they are found. The fibrillar subcomponent displayed protrusions with characteristic ∼ 270 nm periodicity, such that protrusions on neighboring subfibrils were aligned in register. Hence, the banding pattern of mature FLS-type collagen fibrils arises from the in-register alignment of these fibrillar subcomponents. This hierarchical organization observed in FLS-type collagen fibrils is different from that previously reported for native-type collagen fibrils, displaying no supercoiling at the level of organization observed. Proteins 2006.Keywords
Funding Information
- NSERC
- Materials and Manufacturing Onatario Emerging Materials Knowledge.
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