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Protein-Nanocrystal Complexes in Solution. The biological world is filled with examples of intricate enzymatic machinery for complex chemical processes. It may someday be possible to exploit these systems for nanoscale chemistry and assembly. However, the first step will be to study and manipulate the nanomaterial-protein interface in solution. This research effort will form and study the binding affinity between nanostructures and proteins, particular DNA polymerase and chaperones. In one strategy, solution phase assembly will be mediated by DNAp, a dimeric enzyme which recognizes specific sequences of DNA. Thus DNA sequences bound to nanotubes could serve to dictate the assembly pattern around DNAp. For more globular nanostructures, chaperones provide large circular active sites of known chemical structures. Modern drug design programs will be used to explore how nano-object shape, size and surface chemistry can be used to produce specific binding to these sites. In this instance, small polypeptide fragments will serve as the assembly molecules. Binding affinitiy will be evaluate using standard biochemical methods, as well as high resolution NMR in some instances. Smalley, Ma, MacKenzie, Matthews.
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