| Popis: |
Recent amino acid sequence data have revealed that the microfibrils in hard α-keratin contain proteins with highly significant homologies and closely similar structural characteristics to the intermediate filament (IF) proteins known as desmin and vimentin. This result implies that microfibrils in hard α-keratin may be classified as a member of the IF and that the major features of these various filamentous structures are the same. Consequently, data obtained using X-ray diffraction, electron microscopy, amino acid sequence structural analysis and physicochemical techniques have been collated from the hitherto diverse fields of keratin and IF structure and used to formulate a more detailed model for the 7–8 nm diameter filaments than has previously been possible. Two models consisting of four-chain units arranged with the helical symmetry deduced for hard α-keratin1 (Fraser et al. J. Mol. Biol. 1976, 108, 435–452) are in accord with the data. The structural unit comprises an oppositely directed pair of molecules each consisting of a two-stranded parallel-chain coiled-coil rope of length ∼45 nm stabilized by both interchain and intermolecular ionic interactions. For a perfectly regular structure the filament may be likened either to a seven-stranded cable with a supercoil pitch length of about 345 nm (pitch angle ∼2.9°), or a ten-stranded cable (Fraser, R. D. B. and MacRae, T. P. Polymer 1973, 14, 61–67) with a supercoil pitch length of about 1293 nm (pitch angle ∼0.8°). The models also provide some insight into the self-assembly mechanism of the IF. |
