Large-area regular nanodomain patterning in He-irradiated lithium niobate crystals.

Large-area ferroelectric nanodomain patterns, which are desirable for nonlinear optical applications, were generated in previously He-implanted lithium niobate crystals by applying voltage pulses to the tip of a scanning force microscope. The individual nanodomains were found to be of uniform size, which depended only on the inter-domain spacing and the pulse amplitude. We explain this behavior by the electrostatic repulsion of poling-induced buried charges between adjacent domains. The domain patterns were imaged by piezoresponse force microscopy and investigated by domain-selective etching in conjunction with focused ion beam etching followed by scanning electron microscopy imaging. In order to optimize the He-irradiation parameters for easy and reliable nanodomain patterning a series of samples subjected to various irradiation fluences and energies was prepared. The different samples were characterized by investigating nanodomains generated with a wide range of pulse parameters (amplitude and duration). In addition, these experiments clarified the physical mechanism behind the facile poling measured in He-irradiated lithium niobate crystals: the damage caused by the energy loss that takes place via electronic excitations appears to act to stabilize the domains, whereas the nuclear-collision damage degrades the crystal quality, and thus impedes reliable nanodomain generation.

Integrable wide-free-spectral-range Fabry-Perot optical filters using free-standing LiNbO3 thin films.

We demonstrate the use of free-standing thin films of a complex oxide for chip-scale optical filtering. The films are used as low-order etalons with very large free spectral ranges that exceed 6.78 THz (> 50 nm at 1550 nm) and use a small chip area (< 500 microm2) when they are integrated. The films are produced by crystal ion slicing; this process exfoliates a micrometers-thin layer of single-crystal optical material from a bulk parent by means of high-energy-ion implantation. The etalons, which are 10 microm thick with Ag deposited on both surfaces, are integrated into a silica-on-silicon waveguide block.

The binding interface database (BID): a compilation of amino acid hot spots in protein interfaces.

SUMMARY: To make information about protein interactive function easily accessible, we are mining the primary scientific literature for detailed data about protein interfaces. The Binding Interface Database (BID) organizes the vast amount of protein interaction information into tables, graphical contact maps and descriptive functional profiles. Currently data on 170 interacting protein pairs are available with over 1300 mutations described. AVAILABILITY: The BID database is freely available at http://tsailab.org/BID/ To have your protein of interest entered, contact Tiffany Fischer (tiffbrink@neo.tamu.edu) or Jerry Tsai at the email below

Studies on C-phycocyanin from Cyanidium caldarium, a eukaryote at the extremes of habitat.

C-Phycocyanin, a biliprotein, was purified from the red alga, Cyanidium caldarium. This alga grows at temperatures up to 57 degrees C, a very high temperature for a eukaryote, and at pH values down to 0.05. Using the chromophores on C-phycocyanin as naturally occurring reporter groups, the effects of temperature on the stability of the protein were studied by circular dichroism and absorption spectroscopy. The protein was unchanged from 10 to 50 degrees C, which indicates that higher temperatures are not required to cause the protein to be photosynthetically active. At 60 and 65 degrees C, which are above the temperatures at which the alga can survive, the protein undergoes irreversible denaturation. Gel-filtration column chromatography demonstrated that the irreversibility is caused by the dissociation of the trimeric protein to its constitutive polypeptides. Upon cooling, the alpha and beta polypeptides did not reassemble to the trimer. Unlike phycocyanins 645 and 612, the C-phycocyanin does not show a reversible conformational change at moderately high temperatures. At constant temperature, the C-phycocyanin was more stable than a mesophilic counterpart. It is designated a temperature-resistant protein.