Error probability of m-ary fsk with a limiter-discriminator detector in satellite mobile channels

We derive formulae for the error probability of M-ary frequency shift keying with a limiter-discriminator detector in a satellite mobile channel, which includes as special cases the land mobile (Rayleigh) channel and the Gaussian channel. The received signal in this channel is composed of a specular signal, a diffuse signal and white Gaussian noise; hence the composite signal is fading with a Rician envelope. The error probability depends on the signal-to-noise ratio, the power ratio of the specular and diffuse components, the frequency deviation, the Doppler frequency, the maximum Doppler frequency, the time delay between diffuse and specular components, the autocorrelation of the diffuse component and the transfer function of the receive filter. Numerical results are presented as functions of the various parameters. Effects of the receive filter on the signal dependent components are neglected.     

Polymer-dispersed liquid-crystal voltage sensor

We present a novel electric-field and voltage sensor based on the electro-optical properties of polymer-dispersed liquid-crystals (PDLCs). In principle, the transmittance of PDLCs is a nonlinear function of the applied electrical field. To measure an AC field we superposed to it a known DC field. This allowed us to achieve linearization of the PDLC response and to measure transmittance changes independently of the light-intensity level variations. Validation experiments are presented.     

Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis

The actin-activated ATPase activity of Acanthamoeba myosin IC is stimulated 15- to 20-fold by phosphorylation of Ser-329 in the heavy chain. In most myosins, either glutamate or aspartate occupies this position, which lies within a surface loop that forms part of the actomyosin interface. To investigate the apparent need for a negative charge at this site, we mutated Ser-329 to alanine, asparagine, aspartate, or glutamate and coexpressed the Flag-tagged wild-type or mutant heavy chain and light chain in baculovirus-infected insect cells. Recombinant wild-type myosin IC was indistinguishable from myosin IC purified from Acanthamoeba as determined by (i) the dependence of its actin-activated ATPase activity on heavy-chain phosphorylation, (ii) the unusual triphasic dependence of its ATPase activity on the concentration of F-actin, (iii) its Km for ATP, and (iv) its ability to translocate actin filaments. The Ala and Asn mutants had the same low actin-activated ATPase activity as unphosphorylated wild-type myosin IC. The Glu mutant, like the phosphorylated wild-type protein, was 16-fold more active than unphosphorylated wild type, and the Asp mutant was 8-fold more active. The wild-type and mutant proteins had the same Km for ATP. Unphosphorylated wild-type protein and the Ala and Asn mutants were unable to translocate actin filaments, whereas the Glu mutant translocated filaments at the same velocity, and the Asp mutant at 50% the velocity, as phosphorylated wild-type proteins. These results demonstrate that an acidic amino acid can supply the negative charge in the surface loop required for the actin-dependent activities of Acanthamoeba myosin IC in vitro and indicate that the length of the side chain that delivers this charge is important.