The development of periodic nanostructures fabricated by self-assembly of surfactants and block co-polymers has opened up the possibility of generating periodic magnetic nanostructures of types not accessible by self-assembly of nano-particles. The fabrication of mesoporous silica thin films around self-assembled block co-polymers is well established. Common structures for such films are SBA-15 which consists of hexagonal arrays of cylindrical pores and SBA-16 which has face centered arrays of spherical voids. These pores are connected by 1-2 nm thick flaws in the continuous silica phase producing an effectively continuous porous phase. After removal of the block co-polymer template, electrodeposition into the mesoporous silica thin films produces arrays of 5-10 nm diameter nano-wires and nano-particles. We have demonstrated that such materials can be fabricated on a wide range of metal substrates. Characterization by Scanning Electron Microscopies shows that the mesoporous silica is well ordered over micron scale areas. Grazing Incidence Small Angle X-ray Scattering (GISAXS) studies shows diffraction spots, consistent with the entire film being well ordered. GISAXS also shows that the mesoporous silica films survive removal of the template and electrodeposition of nickel and cobalt into the mesoporous silica films. Such films are of interest for their magnetic properties, as the nanophase and scale can be independently varied. Further, the presence of nanowires inside an insulator suggests that these films might also be of interest as the current confining element for Confined Current Path-Current Perpendicular to Plane GMR sensors.

Biochemical and physiological effects of target site resistance to herbicides inhibiting acetolactate synthase (ALS) were evaluated using sulfonylurea-resistant (R) and -susceptible (S) near isonuclear Lactuca sativa ‘Bibb’ lines derived by backcrossing the resistance allele from Lactuca serriola L. into L. sativa. Sequence data suggest that resistance in L. sativa is conferred by a single-point mutation that encodes a proline197 to histidine substitution in Domain A of the ALS protein; this is the same substitution observed in R L. serriola. K mapp (pyruvate) values for ALS isolated from R and S L. sativa were 7.3 and 11.1 mM, respectively, suggesting that the resistance allele did not alter the pyruvate binding domain on the ALS enzyme. Both R and S ALS had greater affinity for 2-oxobutyrate than for pyruvate at the second substrate site. Ratios of acetohydroxybutyrate: acetolactate produced by R ALS across a range of 2-oxobutyrate concentrations were similar to acetohydroxybutyrate: acetolactate ratios produced by S ALS. Specific activity of ALS from R L. sativa was 46% of the specific activity from S L. sativa, suggesting that the resistance allele has detrimental effects on enzyme function, expression, or stability. ALS activity from R plants was less sensitive to feedback inhibition by valine, leucine, and isoleucine than ALS from S plants. Valine, leucine, and isoleucine concentrations were about 1.5 times higher in R seed than in S seed on a per gram of seed basis, and concentrations of valine and leucine were 1.3 and 1.6 times higher, respectively, in R leaves than in S leaves. Findings suggest that the mutation for resistance results in altered regulation of branched-chain amino acid synthesis.