Carla Calvó‐Tusell

This paper investigates how the D614G mutation in SARS-CoV-2 spike protein alters conformational dynamics and allosteric communication, leading to faster RBD opening and increased infectivity.

This study uses molecular dynamics simulations to show how respiratory aerosols create structured microenvironments that influence SARS-CoV-2 stability and spike dynamics.

This study uses molecular dynamics simulations to analyze how mutations in the SHC014-CoV spike protein affect its structural dynamics and allosteric communication, revealing mechanisms that enhance viral entry.

This study models the full-length APOBEC3B structure and finds that NTD-CTD interactions increase active site opening frequency.

This study compares the conformational dynamics of native SARS-CoV-2 Spike protein in virus-like particles to recombinant Spike, finding reduced dynamics in VLP S and implications for epitope display.