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Gold hydrophobization

Eastman and Zhn [52] performed a study of SisN4 tips, subsequently coated with gold and finally with paraffin thin films, adhering to mica. The study was purely qualitative, because they did not have accnrate valnes for either their lever stiffnesses or their tip radii. By enclosing their AEM in a sealed container and controlling the humidity they found that hydrophobic tips show a lower adhesion with a surface expected to have a thin water film, as also observed by Jarvis and Pethica [51]. Surprisingly they did not see any dependence of adhesion on hnmidity for any of their tips. [Pg.37]

FIG. 23 Schematic drawing of using microcontact printing for obtaining hydrophobic areas on a gold-coated substrate. After pattern transfer (a and b), incubation with an S-layer protein solution (c) leads to the formation of a protein monolayer on the hydrophobic areas only. [Pg.382]

Figure 17.3 Anatomy of a redox enzyme representation of the X-ray crystallographic structure of Trametes versicolor laccase III (PDB file IKYA) [Bertrand et al., 2002]. The protein is represented in green lines and the Cu atoms are shown as gold spheres. Sugar moieties attached to the surface of the protein are shown in red. A molecule of 2,5-xyhdine that co-crystallized with the protein (shown in stick form in elemental colors) is thought to occupy the broad-specificity hydrophobic binding pocket where organic substrates ate oxidized by the enzyme. Electrons from substrate oxidation are passed to the mononuclear blue Cu center and then to the trinuclear Cu active site where O2 is reduced to H2O. (See color insert.)... Figure 17.3 Anatomy of a redox enzyme representation of the X-ray crystallographic structure of Trametes versicolor laccase III (PDB file IKYA) [Bertrand et al., 2002]. The protein is represented in green lines and the Cu atoms are shown as gold spheres. Sugar moieties attached to the surface of the protein are shown in red. A molecule of 2,5-xyhdine that co-crystallized with the protein (shown in stick form in elemental colors) is thought to occupy the broad-specificity hydrophobic binding pocket where organic substrates ate oxidized by the enzyme. Electrons from substrate oxidation are passed to the mononuclear blue Cu center and then to the trinuclear Cu active site where O2 is reduced to H2O. (See color insert.)...
Tellurides, on the other hand, are readily floatable in the presence of small quantities of collector, and it is believed that tellurides are naturally hydrophobic. Tellurides from Minnesota (USA) were floated using dithiophosphate collectors, with over 9% gold recovery. [Pg.4]

Ellis, A.V., et al., Hydrophobic anchoring of monolayer-protected gold nanoclusters to carbon nanotubes. Nano Letters, 2003. 3(3) p. 279-282. [Pg.159]


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See also in sourсe #XX -- [ Pg.40 ]




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