Turbulence model study for aerodynamic analysis of the leading edge tubercle wing for low Reynolds number flows.

A turbulence model study was performed to analyze the flow around the Tubercle Leading Edge (TLE) wing. Five turbulence models were selected to evaluate aerodynamic force coefficients and flow mechanism by comparing with existing literature results. The selected models are realizable k-ε, k-ω Shear Stress Transport (SST), ( γ - R e θ ) SST model, Transition k-k l -ω model and Stress- ω Reynolds Stress Model (RSM). For that purpose, the TLE wing model was developed by using the NACA0021 airfoil profile. The wing model is designed with tubercle wavelength of 0.11c and amplitude of 0.03c. Numerical simulation was performed at chord-based Reynolds number of Rec = 120,000. The Computational Fluid Dynamic (CFD) simulation reveals that among the selected turbulence models, Stress- ω RSM estimated aerodynamic forces (i.e. lift and drag) coefficients closest to that of the experimental values followed by realizable k-ε, ( γ - R e θ ) SST model, k-ω SST model and k-k l -ω model. However, at a higher angle of attacks i.e. at 16° & 20° k-ω SST model predicted closest drag and lift coefficient to that of the experimental values. Additionally, the critical observation of pressure contour confirmed that at the lower angle of attack Stress- ω RSM predicted strong Leading Edge (LE) suction followed by realizable k-ε, ( γ - R e θ )SST model, k-ω SST model and k-k l -ω model. Thus, the superiority of Stress- ω RSM in predicting the aerodynamic force coefficients is shown by the flow behavior. In addition to this pressure contours also confirmed that k-k l -ω model failed to predict tubercled wing aerodynamic performance. At higher angles of attacks k-ω SST model estimated aerodynamic force coefficients closest to that of the experimental values, thus k-ω SST model is used at 16° & 20° AoAs. The observed streamline behavior for different turbulence models showed that the Stress- ω RSM model and k-k l -ω model failed to model flow behavior at higher AoAs, whereas k-ω SST model is a better approach to model separated flows that experience strong flow recirculation zone.

Cryo-EM structure of wheat ribosome reveals unique features of the plant ribosomes.

Plants being sessile organisms exhibit unique features in ribosomes, which might aid in rapid gene expression and regulation in response to varying environmental conditions. Here, we present high-resolution structures of the 60S and 80S ribosomes from wheat, a monocot staple crop plant (Triticum aestivum). While plant ribosomes have unique plant-specific rRNA modification (Cm1847) in the peptide exit tunnel (PET), the zinc-finger motif in eL34 is absent, and uL4 is extended, making an exclusive interaction network. We note differences in the eL15-helix 11 (25S) interaction, eL6-ES7 assembly, and certain rRNA chemical modifications between monocot and dicot ribosomes. In eukaryotes, we observe highly conserved rRNA modification (Gm75) in 5.8S rRNA and a flipped base (G1506) in PET. These features are likely involved in sensing or stabilizing nascent chain. Finally, we discuss the importance of the universal conservation of three consecutive rRNA modifications in all ribosomes for their interaction with A-site aminoacyl-tRNA.

Railway track surface faults dataset.

Railway infrastructure maintenance is critical for ensuring safe and efficient transportation networks. Railway track surface defects such as cracks, flakings, joints, spallings, shellings, squats, grooves pose substantial challenges to the integrity and longevity of the tracks. To address these challenges and facilitate further research, a novel dataset of railway track surface faults has been presented in this paper. It is collected using the EKENH9R cameras mounted on a railway inspection vehicle. This dataset represents a valuable resource for the railway maintenance and computer vision related scientific communities. This dataset includes a diverse range of real-world track surface faults under various environmental conditions and lighting scenarios. This makes it an important asset for the development and evaluation of Machine Learning (ML), Deep Learning (DL), and image processing algorithms. This paper also provides detailed annotations and metadata for each image class, enabling precise fault classification and severity assessment of the defects. Furthermore, this paper discusses the data collection process, highlights the significance of railway track maintenance, emphasizes the potential applications of this dataset in fault identification and predictive maintenance, and development of automated inspection systems. We encourage the research community to utilize this dataset for advancing the state-of-the-art research related to railway track surface condition monitoring.

Initiation factor 3 bound to the 30S ribosomal subunit in an initial step of translation.

Bacterial ribosomes require three initiation factors IF1, IF2, and IF3 during the initial steps of translation. These IFs ensure correct base pairing of the initiator tRNA anticodon with the start codon in the mRNA located at the P-site of the 30S ribosomal subunit. IF3 is one of the first IFs to bind to the 30S and plays a crucial role in the selection of the correct start codon and codon: anticodon base pairing. IF3 also prevents the premature association of the 50S subunit of ribosomes and aids in ribosome recycling. IF3 is reported to change binding sites and conformation to ensure translation initiation fidelity. A recent study suggested an initial binding of IF3 CTD away from the P-site and that IF1 and IF2 promote the movement of CTD to the P-site and concomitant movement of NTD. Hence, to visualize the position of IF3 in the absence of any other IFs, we determined cryo-EM structure of the 30S-IF3 complex. The map shows that IF3 is present in an extended conformation with CTD present at the P-site and NTD near the platform even in the absence of IF1 and IF2. Hence, IF3 CTD binds at the P-site and moves away during the accommodation of the initiator tRNA at the P-site in the later steps of translation initiation. Overall, we report the structure of 30S-IF3 which demystifies the starting binding site and conformation of IF3 on the 30S ribosomal subunit.