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Year : 2023, Volume : 13, Issue : 1
First page : ( 14) Last page : ( 16)
Print ISSN : 2319-2186. Online ISSN : 2322-0996. Published online : 2023  09.
Article DOI : 10.5958/2322-0996.2023.00002.9

Investigating protein-ligand interactions for crystal structure of NSP15 endoribonuclease from SARS CoV-2 against caffeine

Singh Keshav1,*, Srivastava Vivek Kumar2, Shukla Ashish2

1Assistant Professor Department of Biotechnology, Raja Balwant Singh Engineering TechnicalCampus, Bichpuri, Agra

2Professor, Department of Biotechnology, Raja Balwant Singh Engineering TechnicalCampus, Bichpuri, Agra

*Corresponding author email: keshav037@skuastkashmir.ac.in

Online published on 9 November, 2023.

Received:  06  ,  2022; :  08  November,  2022; Accepted:  06  December,  2022; :  01  ,  2022.

Abstract

“SARS-CoV-2, the new corona virus that caused the COVID-19 pandemic, has complicated origins and important ramifications. It most likely started in bats, maybe via an intermediary host, and quickly developed, giving rise to many viral strains. (Florian, 2022) Global health and economies are impacted by a wide range of clinical symptoms caused by COVID-19, ranging from minor to severe. This study investigates the binding capability of SARS-CoV-2 against caffeine. In response to this unprecedented global threat, it seeks to improve our understanding of the virus in order to develop stronger pandemic preparedness and response tactics. (Mustafa, 2020) This work offers valuable insights for combating SARS CoV-2 and improving treatment strategies by knowing potential anti- SARS CoV-2 agents specifically against Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2. (Takahiko, 2020)

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Keywords

Bioinformatics, Evolution, Hypothesis, Phylogenomics, Tree.

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