PropertyValue
is ?:annotates of
?:authorAffiliation
  • [\'Institute of Physics, Polish Academy of Sciences, al. Lotnikow 32/46, 02-668 Warsaw, Poland.\', \'Life Science Lab, Institute for Computational Science and Technology, Quang Trung Software City, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City, Vietnam.\', \'Faculty of Physics and Engineering Physics, VNUHCM-University of Science, 227, Nguyen Van Cu Street, District 5, Ho Chi Minh City, Vietnam.\', \'Department of Statistics, University of Oxford, Oxford Protein Bioinformatics Group, Oxford OX1 2JD, United Kingdom.\', \'Department of Chemistry, Penn State University, University Park, Pennsylvania 16802, United States.\', \'Bioinformatics and Genomics Graduate Program, The Huck Institutes of the Life Sciences, Penn State University, University Park, Pennsylvania 16802, United States.\', \'Institute for Computational and Data Sciences, Penn State University, University Park, Pennsylvania 16802, United States.\']
?:citedBy
  • -1
?:creator
?:doi
?:doi
  • 10.1021/acs.jpcb.1c03639
?:hasPublicationType
?:journal
  • The journal of physical chemistry. B
is ?:pmid of
?:pmid
?:pmid
  • 34228472
?:publication_isRelatedTo_Disease
?:rankingScore_SJR
  • -1.0
?:rankingScore_hIndex
  • -1
?:title
  • Electrostatic Interactions Explain the Higher Binding Affinity of the CR3022 Antibody for SARS-CoV-2 than the 4A8 Antibody.
?:type
?:year
  • 2021

Metadata

Anon_0  
expand all