PropertyValue
?:abstract
  • The ability of coronaviruses to infect humans is invariably associated with their binding strengths to human receptor proteins Both SARS-CoV-2, initially named 2019-nCoV, and SARS-CoV were reported to utilize angiotensin-converting enzyme 2 (ACE2) as an entry receptor in human cells To better understand the interplay between SARS-CoV-2 and ACE2, we performed computational alanine scanning mutagenesis on the “hotspot” residues at protein-protein interfaces using relative free energy calculations Our data suggest that the mutations in SARS-CoV-2 lead to a greater binding affinity relative to SARS-CoV In addition, our free energy calculations provide insight into the infectious ability of viruses on a physical basis, and also provide useful information for the design of antiviral drugs
is ?:annotates of
?:creator
?:license
  • unk
?:publication_isRelatedTo_Disease
is ?:relation_isRelatedTo_publication of
?:source
  • WHO
?:title
  • Computational Prediction of Mutational Effects on the SARS-CoV-2 Binding by Relative Free Energy Calculations
?:type
?:who_covidence_id
  • #475
?:year
  • 2020

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