Framework for Real-Time Detection and Identification of possible patients of COVID-19 at public places.

The novel Corona Virus (COVID-19) has become the reason for the world to declare it as a global pandemic, which has already taken many lives from all around the world. This pandemic has become a disaster since the spreading rate from person to person is incredibly high and many techniques have come forth to aid in stopping the infection. Although various types of methods have been put into implementation, the search and suggestions of new approaches to reduce the increasing rate of infection will never come to an end until a vaccine terminates this pandemic. This study focuses on proposing a new framework that is based on Deep Learning algorithms for recognizing the COVID-19 cases, mostly in public places. The algorithms include Background Subtraction for extracting the foreground of thermal images from thermal videos generated by Thermal Cameras through the Thermal Imaging process and the Convolutional Neural Network for detecting people infected with the virus. This automated prototype works in a real-time scenario that helps identify people with the disease and will try to trace it while separating them from having any other contact. This proposal intends to achieve a satisfying growth in determining the real cases of COVID-19 and minimize the spreading rate of this virus to the max, ultimately avoiding more deaths.

Molecular architecture of protein-RNA recognition sites.

The molecular architecture of protein-RNA interfaces are analyzed using a non-redundant dataset of 152 protein-RNA complexes. We find that an average protein-RNA interface is smaller than an average protein-DNA interface but larger than an average protein-protein interface. Among the different classes of protein-RNA complexes, interfaces with tRNA are the largest, while the interfaces with the single-stranded RNA are the smallest. Significantly, RNA contributes more to the interface area than its partner protein. Moreover, unlike protein-protein interfaces where the side chain contributes less to the interface area compared to the main chain, the main chain and side chain contributions flipped in protein-RNA interfaces. We find that the protein surface in contact with the RNA in protein-RNA complexes is better packed than that in contact with the DNA in protein-DNA complexes, but loosely packed than that in contact with the protein in protein-protein complexes. Shape complementarity and electrostatic potential are the two major factors that determine the specificity of the protein-RNA interaction. We find that the H-bond density at the protein-RNA interfaces is similar with that of protein-DNA interfaces but higher than the protein-protein interfaces. Unlike protein-DNA interfaces where the deoxyribose has little role in intermolecular H-bonds, due to the presence of an oxygen atom at the 2' position, the ribose in RNA plays significant role in protein-RNA H-bonds. We find that besides H-bonds, salt bridges and stacking interactions also play significant role in stabilizing protein-nucleic acids interfaces; however, their contribution at the protein-protein interfaces is insignificant.

A protein-RNA docking benchmark (I): nonredundant cases.

We have developed a nonredundant protein-RNA docking benchmark dataset, which is derived from the available bound and unbound structures in the Protein Data Bank involving polypeptide and nucleic acid chains. It consists of nine unbound-unbound cases where both the protein and the RNA are available in the free form. The other 36 cases are of unbound-bound type where only the protein is available in the free form. The conformational change upon complex formation is calculated by a distance matrix alignment method, and based on that, complexes are classified into rigid, semi-flexible, and full flexible. Although in the rigid body category, no significant conformational change accompanies complex formation, the fully flexible test cases show large domain movements, RNA base flips, etc. The benchmark covers four major groups of RNA, namely, t-RNA, ribosomal RNA, duplex RNA, and single-stranded RNA. We find that RNA is generally more flexible than the protein in the complexes, and the interface region is as flexible as the molecule as a whole. The structural diversity of the complexes in the benchmark set should provide a common ground for the development and comparison of the protein-RNA docking methods. The benchmark can be freely downloaded from the internet.