Abstract
Vertebrate collagens constitute a family of at least twelve genetic types that shows remarkable diversity in molecular structure and supramolecular assembly (Mayne & Burgeson, 1987). Types I, II and III collagens assemble in vivo to form fibrils of uniform diameter, near circular cross-section and with a characteristic axial periodicity of 65 to 67 nm (D). Fibrils in vivo are long (several µm) and diameters range from 8 nm to 500 nm, depending on collagen type, species, age and tissue of origin (Parry & Craig, 1984). The mechanisms that control fibril shape and diameter in vivo are poorly understood.
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Hulmes, D.J.S., Mould, A.P., Kadler, K.E., Chapman, J.A., Prockop, D.J. (1989). Procollagen Processing Control of Type I Collagen Fibril Assembly. In: Aebi, U., Engel, J. (eds) Cytoskeletal and Extracellular Proteins. Springer Series in Biophysics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73925-5_53
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DOI: https://doi.org/10.1007/978-3-642-73925-5_53
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