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Title: Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
Authors: Pabisch, S.Puchegger, S.Kirchner, H.O.K.Weiss, I.M.Peterlik, H.
Publishers Version: https://doi.org/10.1016/j.jsb.2010.07.003
Issue Date: 2010
Published in: Journal of Structural Biology Vol. 172 (2010), No. 3
Publisher: San Diego, Calif. : Elsevier
Abstract: The keratin structure in the cortex of peacocks' feathers is studied by X-ray diffraction along the feather, from the calamus to the tip. It changes considerably over the first 5. cm close to the calamus and remains constant for about 1. m along the length of the feather. Close to the tip, the structure loses its high degree of order. We attribute the X-ray patterns to a shrinkage of a cylindrical arrangement of β-sheets, which is not fully formed initially. In the final structure, the crystalline beta-cores are fixed by the rest of the keratin molecule. The hydrophobic residues of the beta-core are locked into a zip-like arrangement. Structurally there is no difference between the blue and the white bird. © 2010 Elsevier Inc.
Keywords: Beta-keratin; Peacock feather; Structure; X-ray diffraction; keratin; article; beta sheet; bird; crystal; feather; hydrophobicity; nonhuman; pavo cristatus; priority journal; protein structure; structure analysis; X ray; X ray diffraction; Animals; beta-Keratins; Feathers; Galliformes; X-Ray Diffraction; Aves; Pavo cristatus
DDC: 570
License: CC BY-NC-ND 3.0 Unported
Link to License: https://creativecommons.org/licenses/by-nc-nd/3.0/
Appears in Collections:Biowissenschaften



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