Analysis performed on the RdRp-Quercetin complex.

<p>A) Distance from the center of mass of Quercetin to RdRp, B) Quercetin RMSD, C) RdRp RMSD, D) the complex RMSD, E) protein RMSF based on the Carbon alpha atoms, F) Radius of Gyration for the protein, G) change in the number of H-bonds, H) the change in the SASA values.</p>

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Bibliographic Details
Main Author:	Ahmed M. Metwaly (9675265) (author)
Other Authors:	Esmail M. El-Fakharany (17345656) (author), Aisha A. Alsfouk (12552755) (author), Ibrahim M. Ibrahim (9269488) (author), Eslam B. Elkaeed (9952518) (author), Ibrahim. H. Eissa (13018476) (author)
Published:	2024
Subjects:	Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Neuroscience Biotechnology Immunology Developmental Biology Cancer Infectious Diseases Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Information Systems not elsewhere classified profile plip studies principal component analysis nine ligands associated flexible alignment experiments div >< p coordinated movements within 81 &# 956 62 &# 177 54 &# 956 200 ns trajectory 149 &# 956 providing valuable insights molecular docking studies ligand interaction fingerprints comprehensive study suggests remdesivir bind similarly remdesivir &# 8217 nine key sars dependent rna polymerase 1 &# 177 2 rdrp inhibitor provided insights molecular dynamics integrated study crystallized ligand vitro </ systems studied selectivity index safety margin rdrp ). promising candidate potent sars inhibiting rdrp including mm hydrogen bonding highly effective effective inhibitor effective anti chemical structure active site 6 ). 46 nm 2 rdrp 2 proteins
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Analysis performed on the RdRp-Quercetin complex.

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