Hydrogen bond occupations of ACE2, SPB25 and designed peptides binding to RBD of the omicron variant.</p
On 26 November 2021, the WHO classified the Omicron variant of the SARS-CoV-2 virus (B.1.1.529 linea...
Hydrogen bonding network analysis of CYP2D6 variants, focus on mutated amino acids.</p
The binding structure of ACE2 (in blue) with RBD (in green) (a), with the mutations (shown in red s...
No. of H-bond and π interactions of ACE2, SPB25 and designed SPB25s involved in binding to Omicron R...
PFED of the best designed 25-mer peptides, SPB25, and ACE2 in binding to Omicron RBD.</p
The binding free energies of ACE2, SPB25 and all designed peptides to RBD of the omicron variant as ...
Only hydrogen bonds with an occupancy higher than 10% are shown. The residue pairs which form hydrog...
The ongoing COVID-19 pandemic continues to infect people worldwide, and the virus continues to evolv...
The number of H- bonds between ACE2 residues with CR1 (A), CR2 (B), and CR3 (C) of the RBD during 7 ...
The RMSD values of all atoms and backbone atoms are shown in black and grey respectively. (TIF)</p
These data are also available at: https://github.com/jbloomlab/SARS-CoV-2-RBD_DMS_Omicron/blob/main/...
A) ΔGbind (MM-GBSA), B) van der Waals energy, C) electrostatic interaction D) polar solvation and E)...
Hydrogen bonds formed on the ACE2&RBD interface for the wildtype (a) and tri-mutant (b) generated fr...
To explore the mechanistic origin that determines the binding affinity of SARS-CoV-2 spike receptor ...
SARS-coronavirus-2 (SARS-CoV2) Omicron variant (B.1.1.529) is of great concern to the world due to m...
On 26 November 2021, the WHO classified the Omicron variant of the SARS-CoV-2 virus (B.1.1.529 linea...
Hydrogen bonding network analysis of CYP2D6 variants, focus on mutated amino acids.</p
The binding structure of ACE2 (in blue) with RBD (in green) (a), with the mutations (shown in red s...
No. of H-bond and π interactions of ACE2, SPB25 and designed SPB25s involved in binding to Omicron R...
PFED of the best designed 25-mer peptides, SPB25, and ACE2 in binding to Omicron RBD.</p
The binding free energies of ACE2, SPB25 and all designed peptides to RBD of the omicron variant as ...
Only hydrogen bonds with an occupancy higher than 10% are shown. The residue pairs which form hydrog...
The ongoing COVID-19 pandemic continues to infect people worldwide, and the virus continues to evolv...
The number of H- bonds between ACE2 residues with CR1 (A), CR2 (B), and CR3 (C) of the RBD during 7 ...
The RMSD values of all atoms and backbone atoms are shown in black and grey respectively. (TIF)</p
These data are also available at: https://github.com/jbloomlab/SARS-CoV-2-RBD_DMS_Omicron/blob/main/...
A) ΔGbind (MM-GBSA), B) van der Waals energy, C) electrostatic interaction D) polar solvation and E)...
Hydrogen bonds formed on the ACE2&RBD interface for the wildtype (a) and tri-mutant (b) generated fr...
To explore the mechanistic origin that determines the binding affinity of SARS-CoV-2 spike receptor ...
SARS-coronavirus-2 (SARS-CoV2) Omicron variant (B.1.1.529) is of great concern to the world due to m...
On 26 November 2021, the WHO classified the Omicron variant of the SARS-CoV-2 virus (B.1.1.529 linea...
Hydrogen bonding network analysis of CYP2D6 variants, focus on mutated amino acids.</p
The binding structure of ACE2 (in blue) with RBD (in green) (a), with the mutations (shown in red s...
DOI
Add to ORKG