A new gm-boosting current reuse CMOs folded cascode LNA

In this paper, a new gain enhancement technique which is recommended for folded cascode LNA structures at low voltage and low power applications is presented. In order to increase power gain, a new modified version of gm-boosting technique is employed which increases the power gain while consuming no extra power. The new topology shares its DC current at the folded stage in order to reduce power dissipation associated with the gm-boosting technique. The proposed technique reduces power dissipation almost 27%, additionally; other parameters such as power gain and noise figure have been slightly improved. In the proposed LNA, power gain and noise figure are15dB and 3.2dB respectively. It consumes 1.3mW under 0.6 supply voltage.

Highly linear low voltage low power CMOS LNA

A highly linear, low voltage, low power, low noise amplifier (LNA) using a novel nonlinearity cancellation technique is presented in this paper. Parallel Inductor (PI) matching is used to increase LNA gain by 3dB at the desired frequency. The linear LNA was designed and simulated in a TSMC 0.18μm CMOS process at 5GHz frequency. By employing the proposed technique, the IIP3 is improved by 12dB in contrast to the conventional folded cascode LNA, reaching −1dBm without having any significant effect on the other LNA parameters such as gain, NF and also power consumption. The proposed LNA also delivers a voltage gain (S21) of 12.25dB with a noise figure of 3.5dB, while consuming only 1.28mW of DC power with a low supply voltage of 0.6V.

Design and optimization of LNA topologies with image rejection filters

An important problem in designing RFIC in CMOS technology is the parasitic elements of passive and active devices that complicate design calculations. This article presents three LNA topologies including cascode, folded cascade, and differential cascode and then introduces image rejection filters for low-side and high-side injection. Then, a new method for design and optimization of the circuits based on a Pareto-based multiobjective genetic algorithm is proposed. A set of optimum device values and dimensions that best match design specifications are obtained. The optimization method is layout aware, parasitic aware, and simulation based. Circuit simulations are carried out based on TSMC 0.18 um CMOS technology by using Hspice.

Haptically-enabled dance visualisation framework for deafblind-folded audience and artists

In this paper we propose a framework for communicating performance art to deaf, blind and deafblind audiences and artists haptically through the sense of touch. This research opens doors for novel artistic trends relying mainly on the sense of touch. The paper investigates the design considerations dictated by solo and group dances as well as stage setup. Implementation scenarios for deafblind audiences and performers are also discussed.

The foldable 'Ottenby' walk-in trap : a handy and efficient wader trap for expedition conditions

We describe the history, construction, and use of a portable walk-in wader trap (i.e., modified Ottenby trap) designed to be used in field expedition conditions. It is rectangular-shaped, 120 × 41 × 32 cm when operational, weighs between 1.5 and 2 kg (depending on materials used) and can be folded flat for easy transportation. It consists of several metal frames filled with fishing net, and has a netted roof attached by an elastic chord. Traps are placed either singly or in groups, with the optimal trapping situation occurring when birds are feeding along some kind of leading line such as the edge of a estuary, lake, or other water body. The trap is highly efficient for waders up to around 100 g, but is also suitable for ground-feeding passerines.

The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis

The folding of proteins is usually studied in dilute aqueous solutions of controlled pH, but it has recently been demonstrated that reversible unfolding can occur in other media. Particular stability is conferred on the protein (folded or unfolded) when the process occurs in ‘protic ionic liquids’ (pILs) of controlled proton activity. This activity (‘effective pH’) is determined by the acid and base components of the pIL and is characterized in the present study by the proton chemical shift of the N–H proton. Here we propose a ‘refoldability’ or ‘refolding index’ (RFI) metric for assessing the stability of folded biomolecules in different solvent media, and demarcate high RFI zones in hydrated pIL media using ribonuclease A and hen egg white lysozyme as examples. Then we show that, unexpectedly, the same high RFIs can be obtained in pIL media that are 90% inorganic in character (simple ammonium salts). This leads us to a conjecture related to the objections that have been raised to ‘primordial soup’ theories for biogenesis, objections that are based on the observation that all the bonds involved in biomacromolecule formation are hydrolyzed in ordinary aqueous solutions unless specifically protected. The ingredients for primitive ionic liquids (NH3, CO, HCN, CO2, and water) were abundant in the early earth atmosphere, and many experiments have shown how amino acids could form from them also. Cyclical concentration in evaporating inland seas could easily produce the type of ambient-temperature, non-hydrolyzing, media that we have demonstrated here may be hospitable to biomolecules, and that may be actually encouraging of biopolymer assembly. Thus a plausible variant of the conventional ‘primordial soup’ model of biogenesis is suggested.

Distinct disulfide isomers of μ-Conotoxins KIIIA and KIIIB block voltage-gated sodium channels

In the preparation of synthetic conotoxins containing multiple disulfide bonds, oxidative folding can produce numerous permutations of disulfide bond connectivities. Establishing the native disulfide connectivities thus presents a significant challenge when the venom-derived peptide is not available, as is increasingly the case when conotoxins are identified from cDNA sequences. Here, we investigate the disulfide connectivity of μ-conotoxin KIIIA, which was predicted originally to have a [C1–C9,C2–C15,C4–C16] disulfide pattern based on homology with closely related μ-conotoxins. The two major isomers of synthetic μ-KIIIA formed during oxidative folding were purified and their disulfide connectivities mapped by direct mass spectrometric collision-induced dissociation fragmentation of the disulfide-bonded polypeptides. Our results show that the major oxidative folding product adopts a [C1–C15,C2–C9,C4–C16] disulfide connectivity, while the minor product adopts a [C1–C16,C2–C9,C4–C15] connectivity. Both of these peptides were potent blockers of NaV1.2 (Kd values of 5 and 230 nM, respectively). The solution structure for μ-KIIIA based on nuclear magnetic resonance data was recalculated with the [C1–C15,C2–C9,C4–C16] disulfide pattern; its structure was very similar to the μ-KIIIA structure calculated with the incorrect [C1–C9,C2–C15,C4–C16] disulfide pattern, with an α-helix spanning residues 7–12. In addition, the major folding isomers of μ-KIIIB, an N-terminally extended isoform of μ-KIIIA identified from its cDNA sequence, were isolated. These folding products had the same disulfide connectivities as μ-KIIIA, and both blocked NaV1.2 (Kd values of 470 and 26 nM, respectively). Our results establish that the preferred disulfide pattern of synthetic μ-KIIIA and μ-KIIIB folded in vitro is 1–5/2–4/3–6 but that other disulfide isomers are also potent sodium channel blockers. These findings raise questions about the disulfide pattern(s) of μ-KIIIA in the venom of Conus kinoshitai; indeed, the presence of multiple disulfide isomers in the venom could provide a means of further expanding the snail’s repertoire of active peptides.