The number of polypeptide chains in the rod domain of bovine epidermal keratin.
The physical properties of the alpha-helix enriched particle obtained by limited proteolysis of epidermal keratin have been examined. Molecular weights in benign and dissociating solvents, hydrodynamic measurements and chemical cross-linking experiments indicate that the particle has four polypeptide chains. It is proposed that the helical particle is assembled from a pair of two-stranded alpha-helical ropes.
D000818:Animals; D002417:Cattle; D007633:Keratins / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012867:Skin; D014357:Trypsin
D046911:Macromolecular Substances; D010446:Peptide Fragments; D007633:Keratins; D014357:Trypsin