Abstract
We have created hybrid devices consisting of nanoscale fabricated inorganic components integrated with and powered by a genetically engineered motor protein.1 We wish to increase the assembly yield and lifetime of these devices through identification, measurement, and improvement of weak internal bonds. Using dynamic force spectroscopy, we have measured the bond rupture force of (histidine)6 on a number of different surfaces as a function of loading rate. The bond sizes, lifetimes, and energy barrier heights were derived from these measurements. We compare the (His)6−nickel bonds to other bonds composing the hybrid device and describe preliminary measurements of the force tolerances of the protein itself. Pathways for improvement of device longevity and robustness are discussed.
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