Abstract
The structure of chicken scale keratin has been investigated by electron microscopy and X-ray diffraction and found to be composed of long 3 nm diameter filaments embedded in an amorphous matrix. The filaments are made up of a helical array of protein chains having a beta conformation and appear to be very similar to those found in feather rachis keratin. They lie in the plane of the scale, grouped into larger undulating fibrils having transverse dimensions of the order of 10 to 20 nm. Within these fibrils the 3 nm filaments are arranged on a two-dimensional hexagonal lattice in contrast to the one-dimensional lattice observed in feather keratin. The highly repetitive portion of the scale sequence [ Eur. J. Biochem. 67 , 283 (1976)], which is absent in feather chains, appears to have a conformation similar to the 3 nm filaments and is thought to be involved in their binding into the two-dimensional lattice.
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