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Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba

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 structu...

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Detalles Bibliográficos
Autores principales: Pabisch, S., Puchegger, S., Kirchner, H.O.K., Weiss, I.M., Peterlik, H.
Formato: Texto
Lenguaje:English
Publicado: Academic Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2977532/
https://www.ncbi.nlm.nih.gov/pubmed/20637873
http://dx.doi.org/10.1016/j.jsb.2010.07.003
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author Pabisch, S.
Puchegger, S.
Kirchner, H.O.K.
Weiss, I.M.
Peterlik, H.
author_facet Pabisch, S.
Puchegger, S.
Kirchner, H.O.K.
Weiss, I.M.
Peterlik, H.
author_sort Pabisch, S.
collection PubMed
description 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.
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spelling pubmed-29775322010-12-06 Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba Pabisch, S. Puchegger, S. Kirchner, H.O.K. Weiss, I.M. Peterlik, H. J Struct Biol Article 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. Academic Press 2010-12 /pmc/articles/PMC2977532/ /pubmed/20637873 http://dx.doi.org/10.1016/j.jsb.2010.07.003 Text en © 2010 Elsevier Inc. https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license
spellingShingle Article
Pabisch, S.
Puchegger, S.
Kirchner, H.O.K.
Weiss, I.M.
Peterlik, H.
Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title_full Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title_fullStr Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title_full_unstemmed Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title_short Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba
title_sort keratin homogeneity in the tail feathers of pavo cristatus and pavo cristatus mut. alba
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2977532/
https://www.ncbi.nlm.nih.gov/pubmed/20637873
http://dx.doi.org/10.1016/j.jsb.2010.07.003
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