Microarray-based in vitro evaluation of DNA oligomer libraries designed in silico.

We report on the microarray-based in vitro evaluation of two libraries of DNA oligonucleotide sequences, designed in silico for applications in supramolecular self-assembly, such as DNA computing and DNA-based nanosciences. In this first study which is devoted to the comparison of sequence motif properties theoretically predicted with their performance in real-life, the DNA-directed immobilization (DDI) of proteins was used as an example of DNA-based self-assembly. Since DDI technologies, DNA computing, and DNA nanoconstruction essentially depend on similar prereguisites, in particular, large and uniform hybridization efficiencies combined with low nonspecific cross-reactivity between individual sequences, we anticipate that the microarray approach demonstrated here will enable rapid evaluation of other DNA sequence libraries.     

Mikrohärteuntersuchungen an Einkristallen der Verbindungen Tl3BX4, (B = V,Nb, Ta; X=S,Se)

Vickers microhardness measurements were performed on single crystals of compounds Tl₃BX₄ (B = V, Nb, Ta; X = S, Se). The anisotropy of the hardness on the (111)-plane was beyond the standard deviation. Besides the load-dependent Vickers hardness HV, the corrected, load-independent hardness HV_c was determined. Tl₃VS₄ showed the highest value of hardness (HV = 66 kp/mm² at 15 p load), the othe compounds differ only slightly in hardness.     

Using atom interferometry to search for new forces

Atom interferometry is a rapidly advancing field and this Letter proposes an experiment based on existing technology that can search for new short distance forces. With current technology it is possible to improve the sensitivity by up to a factor of 10² and near-future advances may be able to rewrite the limits for forces with ranges from 1 mm to 100 m.     

Observation of the decay τ → πv

The decay of the heavy lepton τ into πv has been established using the magnetic detector PLUTO. The branching ratio is determined to be BR(τ→πv)=(9.0 ± 2.9)% with an additional systematic uncertainty of 2.5%. This value is in good agreement with the theoretical prediction.     

Examining the mechanism of action of a kinesin inhibitor using stable isotope labeled inhibitors for cross-linking (SILIC)

It is difficult to determine a chemical inhibitor's binding site in multiprotein mixtures, particularly when high-resolution structural studies are not straightforward. Building upon previous research involving photo-cross-linking and the use of mixtures of stable isotopes, we report a method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC), for mapping a small molecule inhibitor's binding site in its target protein. In SILIC, structure-activity relationship data is used to design inhibitor analogues that incorporate a photo-cross-linking group along with either natural or 'heavy' stable isotopes. An equimolar mixture of these inhibitor analogues is cross-linked to the target protein to yield a robust signature for identifying inhibitor-modified peptide fragments in complex mass spectrometry data. As a proof of concept, we applied this approach to an ATP-competitive inhibitor of kinesin-5, a widely conserved motor protein required for cell division and an anticancer drug target. This analysis, along with mutagenesis studies, suggests that the inhibitor binds at an allosteric site in the motor protein.