Energy-efficient hybrid beamforming for millimeter-wave-based massive multiple-input multiple-output system

The advanced wireless communication system requires abridged energy consumption, enhanced data rate, and good signal coverage. The massive MIMO technology for 5G systems has been developed to accommodate several users simultaneously with superior throughput. The claim for high data rate wireless communication services is expanding quickly as time goes. Thus, the key difficulty is that as the number of users grows, the number of phase shifters grows as well, causing the system to consume more power; as a result, the system's energy efficiency decreases. Hybrid beamforming has recently emerged as an attractive technique for millimeter-wave (mmWave) communication systems. The analog beamformer in the RF domain and digital beamformer in the baseband are coupled through a minimal number of RF chains in hybrid beamforming architecture. Hybrid beamforming utilizes fewer RF (radio frequency) chains than the total number of antennas to have a lower energy consumption design. The hybrid beamforming for a mmWave-based massive MIMO system through different phase shifter selection mechanisms is proposed to achieve the highest energy efficiency for mmWave communications systems. The fully connected with phase shifter selection, sub-connected with phase shifter selection (SPSS), and fully connected and sub-connected with phase shifter selection with halved and doubled switches are considered for this research. The simulation results show the SPSS with halved switch outperforms on energy efficiency.     

Activation of phospholipase D by phosphatidic acid. Enhanced vesicle binding, phosphatidic acid-Ca2+ interaction, or an allosteric effect?

The activity of bacterial phospholipase D (PLD), a Ca2+-dependent enzyme, toward phosphatidylcholine bilayers was enhanced 7-fold by incorporation of 10 mol % phosphatidic acid (PA) in the vesicle bilayer. Addition of other negatively charged lipids such as phosphatidylinositol, phosphatidylmethanol, and oleic acid either inhibited or had no effect on enzyme activity. Only negatively charged lipids with a free phosphate group, phosphatidylinositol 4-phosphate and lyso-PA, had the same effect as PA on enzyme activity. Changes in vesicle curvature and fusion were not the reason for PA activation; rather, a metal ion-induced lateral segregation of PA in the vesicle bilayer correlated with PLD activation. Significant PA activation was also observed with monomer phosphatidylcholine substrate upon the addition of PA vesicles. The PA activation was caused by Ca2+.PA interacting with PLD at an allosteric site other than active site.