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      Using the ring-shaped protein TRAP to capture and confine gold nanodots on a surface.

      Small (Weinheim an Der Bergstrasse, Germany)
      Bacterial Proteins, chemistry, ultrastructure, Binding Sites, Crystallization, methods, Gold, Macromolecular Substances, Materials Testing, Molecular Conformation, Nanospheres, Nanotechnology, Particle Size, Protein Binding, RNA-Binding Proteins, Surface Properties, Transcription Factors

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          Abstract

          The cavity of the toroidal protein TRAP (trp RNA-binding attenuation protein) is modified to capture gold nanodots in solution. By engineering a titanium-binding peptide onto one surface of the ring it is also possible to bind it specifically and tightly to a TiO2 surface. TRAP bound in this way is then used to capture gold nanodots and attach them to prepared surfaces. Gold-protein complexes are observed using atomic force microscopy and transmission electron microscopy. The modified TRAP is used to build gold nanodots into the SiO2 layer of a metal oxide semiconductor. This is the first use of a ring protein, rather than the more commonly used spherical protein cages, to constrain nanodots to a surface. This method is an important addition to the current range of bionanotechnology tools and may be the basis for future, multicomponent electronic devices.

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