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

2010, Pabisch, S., Puchegger, S., Kirchner, H.O.K., Weiss, I.M., Peterlik, H.

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.

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Short range order and topology of binary Ge-S glasses

2022, Pethes, I., Jóvári, P., Michalik, S., Wagner, T., Prokop, V., Kaban, I., Száraz, D., Hannon, A., Krbal, M.

Short range order and topology of GexS100-x glasses over a broad composition range (20 ≤ x ≤ 42 in at%) was investigated by neutron diffraction, X-ray diffraction, and Ge K-edge extended X-ray absorption fine structure (EXAFS) measurements. The experimental data sets were fitted simultaneously in the framework of the reverse Monte Carlo simulation method. It was found that both constituents (Ge and S) satisfy the Mott-rule in all investigated glasses: Ge and S atoms have 4 and 2 neighbours, respectively. The structure of these glasses can be described with the chemically ordered network model: Ge-S bonds are preferred; S-S bonds are present only in S-rich glasses. Dedicated simulations showed that Ge-Ge bonds are necessary in Ge-rich glasses. Connections between Ge atoms (such as edge-sharing GeS4/2 tetrahedra) in stoichiometric and S-rich glasses were analysed. The frequency of primitive rings was also calculated.

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Exploring Structure–Property Relationships of GAGs to Tailor ECM-Mimicking Hydrogels

2018, Zimmermann, Ralf, Werner, Carsten, Sterling, James

Glycosaminoglycans (GAGs) are a class of linear polysaccharides that are ubiquitous in the extracellular matrix (ECM) and on cell surfaces. Due to their key role in development, homeostasis, pathogenesis, and regeneration, GAGs are increasingly used in the design of ECM-mimicking hydrogels to stimulate tissue formation and regenerative processes via specifically orchestrated cell-instructive signals. These applications first and foremost build on the ability of GAGs to effectively bind, protect, and release morphogens. The specificity and strength of morphogen-GAG interactions are largely governed by the number and spatial distribution of negatively charged sulfate groups carried by GAGs. Herein, we summarize a mean-field approach to quantify the density of ionizable groups, GAG concentration, and cross-linking degree of GAG-containing hydrogels on the basis of microslit electrokinetic experiments. We further present and discuss a continuum model of mucosa that accounts for charge regulation by glycan-ion pairing in biological contexts and under conditions of macromolecular crowding. Finally, we discuss the modulation of the morphogen binding and transport in GAG hydrogels by selective desulfation of the GAG component.