| Property | Value |
|---|
|
?:abstract
|
-
The magnified infectious power of the SARS-CoV-2 virus compared to its precursor SARS-CoV is intimately linked to an enhanced ability in the mutated virus to find available hydrogen-bond sites in the host cells. This characteristic is acquired during virus evolution because of the selective pressure exerted at the molecular level. We pinpoint the specific residue (in the virus) to residue (in the cell) contacts during the initial recognition and binding and show that the virusâ â â cell interaction is mainly due to an extensive network of hydrogen bonds and to a large surface of noncovalent interactions. In addition to the formal quantum characterization of bonding interactions, computation of absorption spectra for the specific virusâ â â cell interacting residues yields significant shifts of Δλmax =47 and 66â nm in the wavelength for maximum absorption in the complex with respect to the isolated host and virus, respectively.
|
|
is
?:annotates
of
|
|
|
?:creator
|
|
|
?:journal
|
|
|
?:license
|
|
|
?:publication_isRelatedTo_Disease
|
|
|
is
?:relation_isRelatedTo_publication
of
|
|
|
?:source
|
|
|
?:title
|
-
Binding of SARS-CoV-2 to Cell Receptors: A Tale of Molecular Evolution
|
|
?:type
|
|
|
?:who_covidence_id
|
|
|
?:year
|
|
![[This page as RDF]](https://research.tib.eu/covid-19/static/rdf-icon.gif){kind=icon}