Abstract
The hard keratins of mammals and birds have been extensively studied over recent years and a considerable body of knowledge is now available on the structure and composition of the constituent proteins and of their arrangement within the keratin structure1. Mammalian keratins have a very characteristic structure in which filaments of about 70A diameter are embedded in a non-filamentous matrix composed of sulfur-rich and glycine-tryosine-rich proteins. The filaments are responsible for the α-type X-ray pattern. In contrast avian keratins contain only one family of proteins arranged as small filaments of about 30A diameter which are responsible for a characteristic X-ray pattern, often referred to as the feather type. No sequence homology has been found between avian and mammalian keratin proteins and it is generally considered that they represent separate evolutionary developments.
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© 1987 Plenum Press, New York
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Inglis, A.S., Morton Gillespie, J., Roxburgh, C.M., Whittaker, L.A., Casagranda, F. (1987). Sequence of a Glycine-Rich Protein from Lizard Claw: Unusual Dilute Acid and Heptafluorobutyric Acid Cleavages. In: L’Italien, J.J. (eds) Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1787-6_77
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DOI: https://doi.org/10.1007/978-1-4613-1787-6_77
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