dc.contributor.author
Lauster, Daniel
dc.contributor.author
Haag, Rainer
dc.contributor.author
Ballauff, Matthias
dc.contributor.author
Herrmann, Andreas
dc.date.accessioned
2025-04-04T07:27:17Z
dc.date.available
2025-04-04T07:27:17Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/47163
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-46881
dc.description.abstract
The ectodomain of the Omicron SARS-CoV-2 spike has an increased positive surface charge, favoring binding to the host cell surface, but may affect the stability of the ectodomain. Thermal stability studies identified two transitions associated with the flexibility of the receptor binding domain and the unfolding of the whole ectodomain, respectively. Despite destabilizing effects of some mutations, compensatory mutations maintain ECD stability and functional advantages thus supporting viral fitness.
en
dc.format.extent
8 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
Viral evolution
en
dc.subject
spike protein
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
Balancing stability and function: impact of the surface charge of SARS-CoV-2 Omicron spike protein
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
23
dcterms.bibliographicCitation.doi
10.1038/s44298-025-00104-1
dcterms.bibliographicCitation.journaltitle
npj Viruses
dcterms.bibliographicCitation.volume
3
dcterms.bibliographicCitation.url
https://doi.org/10.1038/s44298-025-00104-1
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie
refubium.funding
Springer Nature DEAL
refubium.note.author
Gefördert aus Open-Access-Mitteln der Freien Universität Berlin.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2948-1767
