Stabilizing antigenic proteins as vaccine immunogens or diagnostic reagents is a stringent
case of protein engineering and design as the exterior surface must maintain recognition by …

The continued emergence of new SARS‐CoV‐2 variants has accentuated the growing need
for fast and reliable methods for the design of potentially neutralizing antibodies (Abs) to …

The long-term side effects and potential development of resistance against existing drugs
make it critical to develop new therapies against COVID-19. However, a crucial barrier to …

The interaction between the receptor-binding domain (RBD) of the SARS-CoV-2 spike
glycoprotein and the ACE2 enzyme is believed to be the entry point of the virus into various …

An unprecedented research effort has been undertaken in response to the ongoing COVID-
19 pandemic. This has included the determination of hundreds of crystallographic structures …

The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein mediates viral
attachment to ACE2 receptor and is a major determinant of host range and a dominant target …

The SARS-CoV-2 pandemic highlights the need for a detailed molecular understanding of
protective antibody responses. This is underscored by the emergence and spread of SARS …

The structure‐based design of antigens holds promise for developing vaccines with higher
efficacy and improved safety profiles. We postulate that abrogation of host receptor …

Protein fold stability likely plays a role in SARS-CoV-2 S-protein evolution, together with
ACE2 binding and antibody evasion. While few thermodynamic stability data are available …

The SARS coronavirus 2 (SARS-CoV-2) spike (S) protein binding to the human ACE2
receptor is the molecular event that initiates viral entry into host cells and leads to infection …