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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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<t>RMSF</t> profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour
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RMSF profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour

Journal: Saudi Pharmaceutical Journal : SPJ

Article Title: Machine learning-guided rational engineering of ACE2-derived peptides for broad-spectrum neutralization of SARS-CoV-2 variants

doi: 10.1007/s44446-026-00073-3

Figure Lengend Snippet: RMSF profiles of the spike RBD and bound peptide during 100 ns molecular dynamics simulations. ( a ) Per-residue RMSF of the spike protein and ( b ) per-residue RMSF of the peptide for SARS-CoV-2 wild type (black) and Omicron variant (red). RMSF values were calculated from the equilibrated portion of independent simulation, with frames sampled every 10 ps. The x-axis indicates residue numbers, and the y-axis represents RMSF values (nm), reflecting residue-level flexibility and dynamic behaviour

Article Snippet: Figure displays the Root Mean Square Fluctuation (RMSF) plots obtained from molecular dynamics simulations.

Techniques: Residue, Variant Assay