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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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Cylinder radius evaluated from the axial 10th layer line (C). Open symbols, white peacock, gray symbols, blue peacock. Note the expanded scale near the calamus, positions 0–30 mm.
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fig7: Cylinder radius evaluated from the axial 10th layer line (C). Open symbols, white peacock, gray symbols, blue peacock. Note the expanded scale near the calamus, positions 0–30 mm.

Mentions: Due to the helical structure, the 10th layer line (C) is split. From the distance between the maxima an approximate radius of the cylindrical helix can be found by searching for the maximum of the appropriate Bessel function (Harford and Squire, 1997). Fig. 7 shows this cylinder radius along the length of the feather evaluated from the 10th layer line. It first increases and then decreases to a final value of  = 1.6 nm, where twice this value – the cylinder diameter – is slightly smaller than the cylinder distance from the first lateral reflection (Fig. 3).


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)

Cylinder radius evaluated from the axial 10th layer line (C). Open symbols, white peacock, gray symbols, blue peacock. Note the expanded scale near the calamus, positions 0–30 mm.
© Copyright Policy
Related In: Results  -  Collection

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

fig7: Cylinder radius evaluated from the axial 10th layer line (C). Open symbols, white peacock, gray symbols, blue peacock. Note the expanded scale near the calamus, positions 0–30 mm.
Mentions: Due to the helical structure, the 10th layer line (C) is split. From the distance between the maxima an approximate radius of the cylindrical helix can be found by searching for the maximum of the appropriate Bessel function (Harford and Squire, 1997). Fig. 7 shows this cylinder radius along the length of the feather evaluated from the 10th layer line. It first increases and then decreases to a final value of  = 1.6 nm, where twice this value – the cylinder diameter – is slightly smaller than the cylinder distance from the first lateral reflection (Fig. 3).

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