15 research outputs found
Low Voltage Totally Free Flexible RF MEMS Switch With Anti-Stiction System
This paper concerns a new design of RF MEMS switch combined with an
innovative process which enable low actuation voltage (<5V) and avoid stiction.
First, the structure described with principal design issues, the corresponding
anti-stiction system is presented and FEM simulations are done. Then, a short
description of the process flow based on two non polymer sacrificial layers.
Finally, RF measurements are presented and preliminary experimental protocol
and results of anti-stiction validation is detailed. Resulting RF performances
are -30dB of isolation and -0.45dB of insertion loss at 10 GHz.Comment: Submitted on behalf of EDA Publishing Association
(http://irevues.inist.fr/handle/2042/16838
Investigation of Tunable Matching Circuits for Multiband 4G Handsets
International audienceTwo antenna designs with tunable matching circuits suitable for 4G mobile terminals are presented. SPDT MEMS switches and tunable capacitors as active components are evaluated in those two different antenna topologies, in scope of the Artemos European project. The target bands include the 4G communication bands, i.e. 700-960MHz as the low-band (LB) and 1.7-2.7GHz as the high-band (HB). In the first design, the antenna operates in the target bands using two SPDT MEMS switches and a two-branched matching network. The second design is a dual-feed structure, where the LB reflection coefficient is tuned using a BST capacitor while the coverage in HB is permanent
Utilization of tunable components for 4G frequency reconfigurable mobile terminal antenna
International audienceIn this paper, two antenna designs using active components are presented for reflection coefficient tunability. The antennas are designed within the scope of the Artemos project and use MEMS switches and BST tunable capacitors internally available in the project. The first antenna uses an SPDT MEMS switch to select between one of the two target frequency bands (700-960MHz and 1.7-2.7GHz). The second antenna uses a tunable capacitor with a tuning range of 2.5-4pF, to frequency tune the reflection coefficient between 700 and 960MHz., The coverage of the 1.7-2.7GHz band is achieved by a monopole antenna who is fed separately
Orthosteric Binding of ρ-Da1a, a Natural Peptide of Snake Venom Interacting Selectively with the α1A-Adrenoceptor
International audienc
Homology modelling of the ρ-Da1a binding site in the α<sub>1A</sub>-AR and the MT7 toxin.
<p>Views from the side of the TM bundle (Panel A), and from the top of the extracellular space (Panel B). F187<sup>5.41</sup>, F193<sup>5.47</sup>, F281<sup>6.44</sup>, M292<sup>6.55</sup>, F308<sup>7.35</sup> in green. D106<sup>3.32</sup> and the double S188<sup>5.42</sup>/S192<sup>5.46</sup> in orange. F86<sup>2.64</sup>, F288<sup>6.51</sup> and F312<sup>7.39</sup> in red. Panel C :3D structure of the three-finger fold MT7 toxin (2vlw) with the four conserved disulfide bridges in red.</p
Receptor affinities for ρ-Da1a (dash lines) and HEAT (solid lines) on mutated α<sub>1A</sub>-ARs.
<p>Binding inhibition curves for <sup>125</sup>I-HEAT binding to WT (200 pM, 0.2 µg, ○), D106<sup>3.32</sup>A (200 pM, 1 µg, □) and F86<sup>2.64</sup>A (1.3 nM, 0.8 µg, •) receptor variants. n = 3–4.</p
Saturation experiments with <sup>125</sup>I-HEAT on receptor variants.
<p>Saturation experiments with <sup>125</sup>I-HEAT on receptor variants.</p
Pharmacological profile of ρ-Da1a binding to various human AR subtypes expressed in eukaryotic cells.
<p>Binding inhibition curves for <sup>3</sup>H-prazosin (2 nM), <sup>3</sup>H-rauwolscine (2 nM) and <sup>3</sup>H-CGP-12177 (6 nM) on hα<sub>1A</sub>- (1 µg, ○), hα<sub>1B</sub>- (3 µg, •), hα<sub>1D</sub>- (29 µg, □), hα<sub>2A</sub>- (140 µg, ◊), hα<sub>2B</sub>- (100 µg, Δ), hα<sub>2C</sub>- (3 µg, x), β<sub>1</sub>- (3 µg,▾) and β<sub>2</sub>-AR (1.5 µg, ▪) with recombinant ρ-Da1a. n = 4.</p
Inhibition of the binding of a series of concentrations of <sup>3</sup>H-prazosin and <sup>125</sup>I-HEAT to α<sub>1A</sub>-AR by ρ-Da1a.
<p>Panel A <sup>3</sup>H-prazosin binding (from 0.2 to 16 nM) inhibited by ρ-Da1a. Panel B <sup>125</sup>I-HEAT binding (from 0.1 to 1.25 nM) inhibited by ρ-Da1a. Panel C and D: Fitting, by the Cheng and Prusoff equation IC<sub>50</sub> = Ki+Ki(L/Kd), of IC<sub>50</sub> values as a function of the radiotracer concentrations.</p