ABSTRACT
The most rapidly expanding type of solar cells are the Perovskite Solar Cells (PSCs), because of its high device performance, ease of synthesis, high open-circuit voltage, and affordability. Despite these advantages, the development of perovskite-based solar cells continues to be impeded by the issues with perovskite stability and the utilization of the hazardous heavy element lead (Pb). The study emphasizes on the bifacial structure that maintains the conventional absorber layer and electron transport layer (ETL) in the optimized PSC structure. This study employs SCAPS software for device simulation to comprehensively analyze how various parameters affect the performance of solar cells. Additionally, doping concentration variation in both ETL and HTL are explored. The simulation reveals that changing device structure from monofacial to bifacial significantly influences PSC performance, demonstrating that optimizing individual layers effectively enhances overall solar cell performance. The optimized structure achieves impressive PSC performance metrics through parametric analysis, such as voltage (VOC) of 1.18 V, fill factor (FF) of 82.24%, current density (JSC) of 27.12 mA/cm2, power conversion efficiency (PCE) of 27.90% for an incident solar spectrum from the ETL side, and power conversion efficiency (PCE) of 19.86% for an incident solar spectrum from the HTL side, the calculated bifaciality factor (BF) for this structure is 71.18%.
ABSTRACT
Two decades after the first report of the plant homolog of the Receptor for Activated C Kinase 1 (RACK1) in cultured tobacco BY2 cells, a significant advancement has been made in the elucidation of its cellular and molecular role. The protein is now implicated in many biological functions including protein translation, multiple hormonal responses, developmental processes, pathogen infection resistance, environmental stress responses, and miRNA production. Such multiple functional roles are consistent with the scaffolding nature of the plant RACK1 protein. A significant advance was achieved when the ß-propeller structure of the Arabidopsis RACK1A isoform was elucidated, thus revealing that its conserved seven WD repeats also assembled into this typical topology. From its crystal structure, it became apparent that it shares the structural platform for the interaction with ligands identified in other systems such as mammals. Although RACK1 proteins maintain conserved Protein Kinase C binding sites, the lack of a bona fide PKC adds complexity and enigma to the nature of the ligand partners with which RACK1 interacts in plants. Nevertheless, ligands recently identified using the split-ubiquitin based and conventional yeast two-hybrid assays, have revealed that plant RACK1 is involved in several processes that include defense response, drought and salt stress, ribosomal function, cell wall biogenesis, and photosynthesis. The information acquired indicates that, in spite of the high degree of conservation of its structure, the functions of the plant RACK1 homolog appear to be distinct and diverse from those in yeast, mammals, insects, etc. In this review, we take a critical look at the novel information regarding the many functions in which plant RACK1 has been reported to participate, with a special emphasis on the information on its currently identified and missing ligand partners.
