PropertyValue
?:abstract
  • A highly infectious coronavirus, SARS-CoV-2, has spread in many countries This virus recognizes its receptor, angiotensin-converting enzyme 2 (ACE2), using the receptor binding domain of its spike protein subunit S1 Many missense mutations are reported in various human populations for the ACE2 gene In the current study, we predict the affinity of many ACE2 variants for binding to S1 protein using different computational approaches The dissociation process of S1 from some variants of ACE2 is studied in the current work by molecular dynamics approaches We study the relation between structural dynamics of ACE2 in closed and open states and its affinity for S1 protein of SARS-CoV-2
is ?:annotates of
?:creator
?:journal
  • Journal_of_Proteome_Research
?:license
  • unk
?:publication_isRelatedTo_Disease
?:source
  • WHO
?:title
  • Studying the effects of ACE2 mutations on the stability, dynamics, and dissociation process of SARS-CoV-2 S1/hACE2 complexes. (Special Issue: Proteomics and its application in pandemic diseases.)
?:type
?:who_covidence_id
  • #960272
?:year
  • 2020

Metadata

Anon_0  
<http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://purl.org/net/provenance/ns#DataItem>
<http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://www.w3.org/2004/03/trix/rdfg-1/Graph>
<http://xmlns.com/foaf/0.1/primaryTopic> <https://research.tib.eu/covid-19/entity/nwv64479>
<http://xmlns.com/foaf/0.1/topic> Anon_0
<http://www.ontologydesignpatterns.org/cp/owl/informationrealization.owl#realizes> <https://research.tib.eu/covid-19/data/entity/nwv64479>
<http://purl.org/net/provenance/ns#createdBy>
Anon_1   (more)
expand all