PJB-2022-377
In-Silico Analysis of Ribosome Inactivating Protein (RIP) of the Cucurbitaceae family
Quratulain Maqsood
Abstract
Ribosome-inactivating proteins (RIPs) are highly active N-glycosidases that depurinate both bacterial and eukaryotic rRNAs, halting protein synthesis during translation. Ribosome inactivating proteins are found in a diverse spectrum of plant species and tissues. Ribosome-inactivating proteins (RIPs) antifungal, antibacterial, antiviral, and insecticidal properties have been connected to plant defense in transgenic plants and in vitro investigations. The ribosome inactivating protein (RIP) peptide in members of the Cucurbitaceae family was physiochemically examined through bioinformatics approaches in this study. It listed the molecular weight, isoelectric point, aliphatic index, extinction coefficient, positive and negative R groups, average hydropathy and instability index of each molecule. Furthermore, their research into the basic architectures of proteins revealed that they are all hydrophobic by nature. SOPMA was used to examine secondary structures. By using Pep Wheel software, the helical wheel structure of ribosome inactivating protein peptide was formed. Phylogenetic analysis and sequence alignment were also carried out. The Swiss model of the protein was also investigated utilising rampage analysis. The data presented may be valuable in establishing a strong foundation for the functional research of ribosome inactivating peptide (RIP) peptides that have been discovered or synthesised experimentally. By investigating these characteristics, as well as how plant RIPs operate, it is feasible to learn more about a novel ribosome inactivating protein (RIP) with potential biological applications.
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