Molecular dynamic simulations reveal detailed spike-ACE2 interactions
The current COVID-19 pandemic has spread throughout the world. Caused by a single-stranded RNA betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is closely related to but much more infectious than the earlier highly pathogenic betacoronaviruses SARS and MERS-CoV, has impacted social, economic, and physical health to an unimaginable extent.
Computational simulations reveal the binding dynamics between human ACE2 and the receptor binding domain of SARS-CoV-2 spike protein
Molecular dynamic simulation suggests stronger interaction of Omicron-spike with ACE2 than wild but weaker than Delta SARS-CoV-2 can be blocked by engineered S1-RBD fraction
Molecular Interaction And Inhibition Of SARS-CoV-2 Binding, 54% OFF
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Molecular Interaction And Inhibition Of SARS-CoV-2 Binding, 54% OFF
Computational biophysical characterization of the SARS-CoV-2 spike protein binding with the ACE2 receptor and implications for infectivity - Computational and Structural Biotechnology Journal
Unraveling SARS-Cov-2 spike protein conformational dynamics under the influence of electric fields - NHR4CES
Mutational landscape and in silico structure models of SARS-CoV-2 spike receptor binding domain reveal key molecular determinants for virus-host interaction, BMC Molecular and Cell Biology
PDF) Dynamics of the ACE2–SARS-CoV-2/SARS-CoV spike protein interface reveal unique mechanisms
A molecular dynamics simulation study of the ACE2 receptor with screened natural inhibitors to identify novel drug candidate against COVID-19 [PeerJ]
In silico comparison of SARS-CoV-2 spike protein-ACE2 binding affinities across species and implications for virus origin
Molecular dynamic simulation suggests stronger interaction of Omicron-spike with ACE2 than wild but weaker than Delta SARS-CoV-2 can be blocked by engineered S1-RBD fraction
Comparison between experimental and modeled SARS-CoV-2 Spike-Ace2
Molecular Interaction And Inhibition Of SARS-CoV-2 Binding, 54% OFF
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level