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

Pabisch S, Puchegger S, Kirchner HO, Weiss IM, Peterlik H - J. Struct. Biol. (2010)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: University of Vienna, Faculty of Physics, Strudlhofgasse 4, A-1090 Vienna, Austria.

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Offset angle between the axial reflection (A) (length direction of keratin filament) and the lateral reflection (B) (perpendicular direction of the keratin filament). Open symbols, white peacock, gray symbols, blue peacock. The abscissa is broken to allow for the strong change in the region close to the calamus, positions 0–30 mm.
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fig6: Offset angle between the axial reflection (A) (length direction of keratin filament) and the lateral reflection (B) (perpendicular direction of the keratin filament). Open symbols, white peacock, gray symbols, blue peacock. The abscissa is broken to allow for the strong change in the region close to the calamus, positions 0–30 mm.

Mentions: Another significant change concerns the angle between the first axial (A) and lateral (B) reflections, Fig. 6. It stems from the orientation of the keratin filaments along the long and the perpendicular axis, respectively. The angle strongly decreases over the first 50 mm of the rachis, beyond it remains constant at a value of 90°. This clearly indicates that the arrangement of the filaments at first is not perpendicular to their long axis, but differently inclined, until the length axis of the filament is perfectly perpendicular to their arrangement in the lateral direction.


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

Pabisch S, Puchegger S, Kirchner HO, Weiss IM, Peterlik H - J. Struct. Biol. (2010)

Offset angle between the axial reflection (A) (length direction of keratin filament) and the lateral reflection (B) (perpendicular direction of the keratin filament). Open symbols, white peacock, gray symbols, blue peacock. The abscissa is broken to allow for the strong change in the region close to the calamus, positions 0–30 mm.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2977532&req=5

fig6: Offset angle between the axial reflection (A) (length direction of keratin filament) and the lateral reflection (B) (perpendicular direction of the keratin filament). Open symbols, white peacock, gray symbols, blue peacock. The abscissa is broken to allow for the strong change in the region close to the calamus, positions 0–30 mm.
Mentions: Another significant change concerns the angle between the first axial (A) and lateral (B) reflections, Fig. 6. It stems from the orientation of the keratin filaments along the long and the perpendicular axis, respectively. The angle strongly decreases over the first 50 mm of the rachis, beyond it remains constant at a value of 90°. This clearly indicates that the arrangement of the filaments at first is not perpendicular to their long axis, but differently inclined, until the length axis of the filament is perfectly perpendicular to their arrangement in the lateral direction.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: University of Vienna, Faculty of Physics, Strudlhofgasse 4, A-1090 Vienna, Austria.

Show MeSH