Analysis and Design of CMOS Radio-Frequency Power Amplifiers

The continuous advancement of semiconductor technologies, especially CMOS technology, has enabled exponential growth of the wireless communication industry. This explosive growth in turn has completely changed people’s lives. The CMOS feature size scale down greatly benefits digital logic integrations, which result in more powerful, versatile, and economical digital signal processing. Further research and development has pushed analog, mixed-signal, and even radio-frequency (RF) circuit blocks to be implemented and integrated in CMOS. Future generations of wireless communication call for even further level of integration, and as of now, the only circuit block that is rarely integrated in CMOS along with other parts of the system is the power amplifier (PA). Due to the fact that the PA in a wireless communication system is the most power-hungry circuit block, the integration of RF PA in CMOS would potentially not only save the cost of the wireless communication system real estate, but also reduce power consumption since die-to-die connection loss can be eliminated. RF PA design involves handling large amounts of voltage and current at the radio frequencies, which in the present wireless communication standards are in the range of giga-hertz. Therefore, a good understanding of many aspects related to RF PA design is necessary. Theoretical analysis of the communication system, nonlinear effects of the PA, as well as the impedance matching network is systematically presented. The analysis of the nonlinear effects proposes a formal mathematical description of the multitone nonlinearity, and through its relationship with two-tone test, the proposed PA design methodology would greatly reduce the design time while improving the design accuracy. A thorough analysis of the available architecture and design techniques for efficiency and linearity enhancement of RF PA shows that despite tremendous amounts of research and development into this topic, the fundamental tradeoff between the two still limits the RF PA implementation largely within SiGe, GaAs, and InP technologies. A RF PA for Wideband Code-Division Multiple Access (WCDMA) application standard is proposed, designed, and implemented in CMOS that demonstrates the proposed segmentation technique that resolved the main tradeoff between power efficiency and linearity. The innovative architecture developed in this work is not limited to applications in the WCDMA communication protocol or the CMOS technology, although CMOS implementation would take advantage of the readily available digital resources

A. Schematic representation of a <i>T</i>. <i>gondii</i> tachyzoite highlighting the localization and composition of the three glideosomes.

<p>B. Localization of three glideosomes by immunofluorescence using the endogenously tagged TgGAP70 and TgGAP80 and the anti-TgGAP45 antibodies. Scale bars: 2 μm. C. Relocalization of MycMyoC to the periphery of the tachyzoite in addition to its basal localization in absence of TgMyoA in the MycMyoC-cKD/MyoA-KO strain. Scale bars: 2 μm.</p

Summary of the phenotype and adaptation observed in the cell lines discussed in this review according to the technology used to investigate the function of the corresponding gene.

<p>Summary of the phenotype and adaptation observed in the cell lines discussed in this review according to the technology used to investigate the function of the corresponding gene.</p

Schematic interpretation of host–parasite interactions of epicellular piscine cryptosporidians and coccidians.

<p>Monopodial stage of <i>Cryptosporidium molnari</i> with the detail of feeder organelle (inset) (A; modified from Alvarez-Pellitero P, Palenzuela O, Sitjà-Bobadilla A. 2002. <i>Cryptosporidium molnari</i> n. sp. (Apicomplexa: Cryptosporidiidae) infecting two marine fish species, <i>Sparus aurata</i> L. and <i>Dicentrarchus labrax</i> L. Figs 23 and 30. International Journal for Parasitology 32: 1007–1021. Elsevier 2002), <i>Cryptosporidium villithecus</i> (B; adapted from Landsberg and Paperna, 1986), <i>Goussia janae</i> (C; adapted from Lukeš J, Starý V. 1992. Ultrastructure of life cycle stages of <i>Goussia janae</i> (Apicomplexa, Eimeriidae) and X-ray microanalysis of accompanying precipitates. Canadian Journal of Zoology, 70 (12): 2382–2397, 2008 Canadian Science Publishing or its licensors. Reproduced with permission), <i>Eimeria anguillae</i> (D), <i>Goussia spraguei</i> (E; adapted from A new species of <i>Goussia</i> (Apicomplexa, Coccidia) in the kidney tubules of the cod, <i>Gadus morhua</i> L. Morrison CM, Poynton SL. Journal of Fish Diseases 12 (6). 1989. John Wiley & Sons, Inc. <a href="http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2761.1989.tb00564.x/abstract" target="_blank">http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2761.1989.tb00564.x/abstract</a>), <i>Eimeria puytoraci</i> (F), <i>Eimeria vanasi</i> with the detail of its protrusions into the host cell cytoplasm (inset) (G; adapted from Paperna, (1991). Kim and Paperna (1992)); Spider-like stage of <i>Goussia pannonica</i> (H; adapted from Life cycle of <i>Goussia pannonica</i> (Molnár, 1989) (Apicomplexa, Eimeriorina), an extracytoplasmic coccidium from the white bream <i>Blicca bjoerkna</i>. Lukeš J. Journal of Protozoology 39 (4). 1992 John Wiley & Sons, Inc. <a href="http://onlinelibrary.wiley.com/doi/10.1111/j.1550-7408.1992.tb04836.x/abstract" target="_blank">http://onlinelibrary.wiley.com/doi/10.1111/j.1550-7408.1992.tb04836.x/abstract</a>). In all figures, the scale bar is 1 μm, with the exception of insets (0.2 μm in A and 0.3 μm in G).</p

Schematic interpretation of mechanisms of host invasion by the epicellular (EPCL) piscine cryptosporidians and coccidians.

<p>(<b>A</b>) Invasion of host cell by <i>Cryptosporidium</i> spp. Zoite penetrates among the microvilli (A1), which eventually surround and enclose it within the parasitophorous sac (A2–A3). Finally, the feeder organelle is formed (A4). (<b>B)</b> The invasion mechanism resulting in the formation of monopodial stages of an EPCL coccidium. The beginning of invasion, until the enclosure of the parasite by the host cell membrane, is similar as in A (B1), but the feeder organelle does not form (B2) and the attachment remains monopodial (B3–B4). (<b>C</b> and <b>D)</b> Two possible mechanisms of formation of the spider-like EPCL stages. (<b>C</b>) The zoite settles down and fuses with the apical part of the microvillus (C1) and its growth progressively extends to the neighbouring microvilli (C2). Contact between the infected microvillar membrane and the membranes of other microvilli (C3) results in their fusions (C4), thus attaching the parasite to the host cell via additional region(s). (<b>D)</b> The zoite settles down at the microvillar zone laterally (D1), inducing fusion of non-neighbouring microvilli and its enclosure (D2–D3), thus forming a spider-like stage attached to the host cell (or more cells) in several regions (D4).</p

The MyoC-glideosome is dispensable in tachyzoites.

<p>A. No growth defect was detected 7 days post-invasion by plaque assays performed with Ku80-KO and GAP80-KO strains. B. In absence of GAP80, endogenous MyoC and IAP1 (KI-MyoC-3Ty and KI-IAP1-3Ty) are still localized to the basal polar ring. Scale bars: 2 µm. C. Co-IP experiments performed with anti-GAP45 antibodies on Ku80-KO and GAP80-KO strains after metabolic labeling with [³⁵S]-methionine/cysteine. D. Plaque assays performed with Ku80-KO and IAP1-KO cell lines and fixed after 7 days. E. Immunofluorescence assays performed on intracellular parasites showing that in absence of IAP1, MyoC and GAP80 (MycMyoC-iKO and KI-GAP80Ty) are not localized to the basal polar ring anymore. Scale bars: 2 µm. F. Western blot analysis of total extract of parasites expressing KI-GAP80Ty in 3 different backgrounds. G. Localization of GAP45 in Ku80-KO, GAP80-KO and IAP1-KO cell lines relatively to GAP40Ty showing that in absence of IAP1 or GAP80, GAP45 staining goes further down to the basal complex as illustrated by the magnifications of the posterior poles and the RGB profile plots determined using ImageJ along the arrow. Scale bars: 2 µm. Little arrows point to the apical pole of the parasites while arrowheads point to the posterior pole.</p

Summary of the phenotypes observed in this study.

1<p>For GAP45-iKO, values are the mean of the assays presented in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004504#ppat-1004504-g005" target="_blank">figures 5</a> and <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004504#ppat-1004504-g006" target="_blank">6</a>;</p>2<p>Gliding refers to deposited trails, + and – indicate if trails or no trails were visualized, respectively.</p><p>Summary of the phenotypes observed in this study.</p

MyoC is dispensable in tachyzoites.

<p>A. Localization of endogenous MyoC N-terminally Myc-tagged (MycMyoC-iKO) and of endogenous truncated MyoC (KI-MyoC-ΔN&T-3Myc) expressed in KI-GAP80Ty or KI-IAP1-3Ty. Scale bars: 2 µm. B. Total lysates from parasites expressing MycMyoC-iKO and KI-MyoC-ΔN&T-3Myc/KI-GAP80Ty were analyzed by western blot with anti-Myc antibodies. Parasites expressing KI-GAP80Ty were loaded as a control and CAT as a loading control. C. Plaque assays performed with Ku80-KO, KI-GAP80Ty, MyoC-ΔN&T-3Myc/KI-GAP80Ty, MyoC-KO/KI-GAP80Ty cell lines and fixed after 7 days. No defect in the lytic cycle was observed. D. Co-IP experiments performed with anti-Ty antibodies on cell lines metabolically labeled and expressing KI-GAP80Ty in a wild type and in a MyoC-KO background.</p

A non-functional MyoC fails to incorporate into the basal glideosome complex.

<p>A. Localization of MycMyoC-iKO and MycMyoC-K205E-iKO in dividing parasites stained with an IMC marker shows that the mutated MyoC is not incorporated in the mature parasites. Scale bars: 2 µm. B. Western blot analysis of total extract of intracellular parasites expressing MycMyoC-iKO and MycMyoC-K205E-iKO. The mutated MyoC is never detected with anti-Myc antibodies.</p

Two myosin light chains shared between two motors.

<p>A. The solubility of GAP80 constructs (KI-GAP80Ty and GAP80Ty) was assessed by fractionation after extraction in PBS, PBS/NaCl, PBS/Na₂CO₃ or PBS/Triton X-100. Their distribution in different fractions was assessed by western blot using anti-Ty antibodies and the soluble catalase (CAT) as control for the correct fractionation. B. Parasites stably expressing a second copy of GAP45Ty and GAP80Ty were labeled with [³⁵S]-methionine/cysteine and subjected to co-IP with anti-Ty antibodies. Eluted proteins were visualized by autoradiography. A protein above 130 kDa was additionally found in GAP80Ty elution and identified as MyoC. C. Metabolically labeled parasites endogenously Ty-tagged at the <i>GAP45</i>, <i>GAP80</i> or <i>MyoC</i> locus have been subjected to co-IP with anti-Ty antibodies. The black circles correspond to the respective bait. The same elution fractions were analyzed by western blot using anti-GAP40 and anti-GAP45 antibodies, respectively. The asterisks indicate the Ig heavy chains that cross-react with the antibodies. D. Autoradiography of labeled parasites stably expressing a second copy of MLC1Ty after co-IP experiment with anti-Ty antibodies. E. Localization of the endogenous MyoC in a ring-like structure at the basal pole of mature parasites and late stage daughter cells using anti-Ty and anti-IMC1 antibodies. Scale bars: 2 µm. F. Autoradiography of labeled parasites stably expressing a Ty-tagged version of the endogenous ELC1 (KI-ELC1-3Ty) after co-IP performed with anti-Ty antibodies. Scale bars: 2 µm. G. Localization of the endogenously tagged ELC1, MLC1 and GAP40 and of loxP-TyMyoA assessed in intracellular parasites using anti-Ty and anti-GAP45 antibodies. Arrowheads point to the basal end of the parasites that are also presented in the magnifications.</p