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- https://bio.libretexts.org/Courses/Coastline_College/Book-_Cells_-_Molecules_and_Mechanisms_(Wong)/07%3A_Membrane_Boundaries_and_Capturing_Energy/7.05%3A_Cytoskeleton/7.5.10%3A_Extracellular_Matrix_and_Cell_Adhesion/7.5.10.04%3A_FibronectinsFibronectin and laminin are significantly smaller than either collagens or proteoglycans, and play different roles in the extracellular matrix. Fibronectin is formed by the joining of two similar poly...Fibronectin and laminin are significantly smaller than either collagens or proteoglycans, and play different roles in the extracellular matrix. Fibronectin is formed by the joining of two similar polypeptide subunits via a pair of disulfide bonds near the C-terminal of each (fig. 5). Each subunit is arranged as a linear sequence of 30 functional domains (varies slightly by species). Within each subunit, each domain acts as a semi-independent unit with respect to secondary and even tertiary struc
- https://bio.libretexts.org/Bookshelves/Cell_and_Molecular_Biology/Book%3A_Cells_-_Molecules_and_Mechanisms_(Wong)/13%3A_Extracellular_Matrix_and_Cell_Adhesion/13.04%3A_FibronectinsFibronectin and laminin are significantly smaller than either collagens or proteoglycans, and play different roles in the extracellular matrix. Fibronectin is formed by the joining of two similar poly...Fibronectin and laminin are significantly smaller than either collagens or proteoglycans, and play different roles in the extracellular matrix. Fibronectin is formed by the joining of two similar polypeptide subunits via a pair of disulfide bonds near the C-terminal of each (fig. 5). Each subunit is arranged as a linear sequence of 30 functional domains (varies slightly by species). Within each subunit, each domain acts as a semi-independent unit with respect to secondary and even tertiary struc
