Nanowires have been taken much attention as a nanoscale building block, which can perform the excellent mechanical function as an electromechanical device. Here, we have performed atomic force microscope (AFM)-based nanoindentation experiments of silicon nanowires in order to investigate the mechanical properties of silicon nanowires. It is shown that stiffness of nanowires is well described by Hertz theory and that elastic modulus of silicon nanowires with various diameters from ~100 to ~600 nm is close to that of bulk silicon. This implies that the elastic modulus of silicon nanowires is independent of their diameters if the diameter is larger than 100 nm. This supports that finite size effect (due to surface effect) does not play a role on elastic behavior of silicon nanowires with diameter of >100 nm.

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Multimode microbolometers for wavelength-selective infrared detection have been designed using a Genetic Algorithm and an electromagnetic model of the planar antenna. Wavelength selectivity can be varied by changing the distance to a tuning mirror, or by changing only lithographically drawn parameters, with bandwidth narrower than Fabry-Perot microbolometers. The design of a three color system covering the 7-14 micron band is presented.

Quantitative understanding of the mechanical behavior of biological liquid crystals such as proteins is essential for gaining insight into their biological functions, since some proteins perform notable mechanical functions. Recently, single-molecule experiments have allowed not only the quantitative characterization of the mechanical behavior of proteins such as protein unfolding mechanics, but also the exploration of the free energy landscape for protein folding. In this work, we have reviewed the current state-of-art in single-molecule bioassays that enable quantitative studies on protein unfolding mechanics and/or various molecular interactions. Specifically, single-molecule pulling experiments based on atomic force microscopy (AFM) have been overviewed. In addition, the computational simulations on single-molecule pulling experiments have been reviewed. We have also reviewed the AFM cantilever-based bioassay that provides insight into various molecular interactions. Our review highlights the AFM-based single-molecule bioassay for quantitative characterization of biological liquid crystals such as proteins.

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Label-free detection of biomolecular interactions was performed using BioFET(Biologically sensitive Field-Effect Transistor) and SPR(Surface Plasmon Resonance). Qualitative information on the immobilization of an anti-IgG and antibody-antigen interaction was gained using the SPR analysis system. The BioFET was used to explore the pI value of the protein and to monitor biomolecular interactions which caused an effective charge change at the gate surface resulting in a drain current change. The results show that the BioFET can be a useful monitoring tool for biomolecular interactions and is complimentary to the SPR system.