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Literature summary for 3.4.17.23 extracted from

  • Gutgsell, A.; Gunnarsson, A.; Forssen, P.; Gordon, E.; Fornstedt, T.; Geschwindner, S.
    Biosensor-enabled deconvolution of the avidity-induced affinity enhancement for the SARS-CoV-2 spike protein and ACE2 interaction (2022), Anal. Chem., 94, 1187-1194 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
analysis analysis of the interaction between ACE2 and SARS-CoV-2 spike protein using a surface plasmon resonance-based assay that reduces the heterogeneity introduced from multivalent binding interactions to enable the determination of the kinetic rate constants for multivalent binding interactions. Controlling the sensor surface heterogeneity enables the deconvolution of the avidity-induced affinity enhancement for the SARS-CoV-2 spike protein and ACE2 interaction Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
87000
-
 gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BYF1
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Homo sapiens

Subunits

Subunits Comment Organism
monomer 1 * 87000, mass photometry, purified ACE2 ectodomain Homo sapiens

General Information

General Information Comment Organism
physiological function the SARS-CoV-2 spike protein binds to ACE2. The spike protein samples at least four different conformational states, of which three are defined via different ACE2-bound states Homo sapiens