Abstract
A model for the structural arrangements of the protein chains in α-keratin has been proposed on the basis of the diffraction pattern of porcupine quill tips. The model implies that the protein chains are basically of the α-helix configuration but are supercoiled and packed in five concentric layers. The supercoiling in the different layers makes one turn in 198 Å along the axis of the tonofilament. The number of chains in the different layers are 3, 7, 10, 16, and 19. This arrangement that is based on the diffraction pattern gives a diameter of the tonofilament that is in agreement with electron microscopic data.
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