In-silico computational strategies for structure-based characterization of the fusion protein of Nipah henipavirus

Throughout history, viral epidemics of varying frequency and intensity have been responsible for inducing panic and causing widespread damage. The Nipah virus has one of the highest rates of fatalities of any infectious disease in the world. There have been cases when severe respiratory distress has resulted in death, and it is known that these cases can cause encephalitis. The appearance of the virus and its ability to spread is affected by several factors. Several strategies have been created to raise awareness about the need for personal hygiene and enhance surveillance within the contaminated zone. This work aimed to determine the characteristics of a previously unidentified protein linked with the fusion of Nipah henipavirus particles. The protein's secondary structure comprises helix, sheet, turn, and secondary coil structures. The protein is a fusion protein. In addition, the estimated Ramachandran plot provided evidence of the accuracy of the modeled protein structure. This accuracy was then verified by the Z-score-based and local model quality evaluation methods. It is possible to think of the protein as a target for developing prospective therapeutic and vaccine candidates directed against the protein to fight viral infections.