Doping-insensitive density-of-states suppression in polycrystalline iron-based superconductor SmO1−x_{1-x}Fx_{x}FeAs

We investigated the temperature dependence of the density-of-states in the iron-based superconductor SmO_1-xF_xFeAs (x=0, 0.12, 0.15, 0.2) with high resolution angle-integrated photoemission spectroscopy. The density-of-states suppression is observed with decreasing temperature in all samples, revealing two characteristic energy scales (10meV and 80meV). However, no obvious doping dependence is observed. We argue that the 10meV suppression is due to an anomalously doping-independent normal state pseudogap, which becomes the superconducting gap once in the superconducting state; and alert the possibility that the 80meV-scale suppression might be an artifact of the polycrystalline samples.Comment: 4 pages, 4 figure

Strategies for Controlled Placement of Nanoscale Building Blocks

The capability of placing individual nanoscale building blocks on exact substrate locations in a controlled manner is one of the key requirements to realize future electronic, optical, and magnetic devices and sensors that are composed of such blocks. This article reviews some important advances in the strategies for controlled placement of nanoscale building blocks. In particular, we will overview template assisted placement that utilizes physical, molecular, or electrostatic templates, DNA-programmed assembly, placement using dielectrophoresis, approaches for non-close-packed assembly of spherical particles, and recent development of focused placement schemes including electrostatic funneling, focused placement via molecular gradient patterns, electrodynamic focusing of charged aerosols, and others

Internet resources for proteins associated with drug therapeutic effects, adverse reactions and ADME

10.1016/S1359-6446(03)02742-9Drug Discovery Today812526-529DDTO

A novel conotoxin from <i>Conus betulinus</i>, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator

A novel conotoxin, kappa-conotoxin (kappa-BtX), has been purified and characterized from the venom of a worm-hunting cone snail, Conus betulinus. The toxin, with four disulfide bonds, shares no sequence homology with any other conotoxins. Based on a partial amino acid sequence, its cDNA was cloned and sequenced. The deduced sequence consists of a 26-residue putative signal peptide, a 31-residue mature toxin, and a 13-residue extra peptide at the C terminus. The extra peptide is cleaved off by proteinase post-processing. All three Glu residues are gamma-carboxylated, one of the two Pro residues is hydroxylated at position 27, and its C-terminal residue is Pro-amidated. The monoisotopic mass of the toxin is 3569.0 Da. Electrophysiological experiments show that: 1) among voltage-gated channels;, K-BtX is a specific modulator of K+ channels; 2) among the K channels, kappa-BtX specifically up-modulates the Ca2+- and voltage-sensitive BK channels (252 47%); 3) its EC50 is 0.7 nm with a single binding site (Hill = 0.88); 4) the time constant of wash-out is 8.3 s; and 5) kappa-BtX has no effect on single channel conductance, but increases the open probability of BK channels. It is concluded that kappa-BtX is a novel specific biotoxin against BK channels