PropertyValue
?:abstract
  • In this comutational work a hybrid quantum mechanics/molecular mechanics approach, the MD-PMM approach, is used to investigate the proton transfer reaction the activates the catalytic activity of SARS-CoV-2 main protease. The proton transfer thermodynamics is investigated for the apo ensyme (i.e., without any bound substrate or inhibitor) and in the presence of a inhibitor, N3, which was previously shown to covalently bind SARS-CoV-2 main protease.
is ?:annotates of
?:creator
?:doi
  • 10.26434/chemrxiv.13200227
?:doi
?:externalLink
?:journal
  • ChemRxiv
?:license
  • cc-by-nc-nd
?:pdf_json_files
  • document_parses/pdf_json/e92dbd62f33a7f25ae6b1c3fa19f0050077f4caa.json
?:pmcid
?:pmid
?:pmid
  • 33200115
?:publication_isRelatedTo_Disease
is ?:relation_isRelatedTo_publication of
?:sha_id
?:source
  • PMC
?:title
  • Tuning Proton Transfer Thermodynamics in SARS-Cov-2 Main Protease: Implications for Catalysis and Inhibitor Design
?:type
?:year
  • 2020-11-06

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/zyghu7wk>
<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/zyghu7wk>
<http://purl.org/net/provenance/ns#createdBy>
Anon_1   (more)
expand all