Distribution of secondary structure along the fibronectin molecule.
30-kDa, 50-kDa and 70-kDa gelatin-binding, 60-kDa central and 60-65-kDa heparin-binding fragments were produced by trypsin digestion of fibronectin. The secondary structure of the fragments was studied by circular dichroism and quantitative infrared spectroscopy. The structure of the 70-kDa gelatin-binding, 60-kDa central and 60-65-kDa heparin-binding fragments in solution appeared to be very close to that in the intact fibronectin. The content of the antiparallel beta-form, the only element of the secondary structure in all the fragments studied, was shown to be 30-35%.
D001665:Binding Sites; D002942:Circular Dichroism; D005353:Fibronectins / Q000302:isolation & purification*; D006493:Heparin / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet
D005353:Fibronectins; D010446:Peptide Fragments; D006493:Heparin