D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes
Fiona L. Kearns, Anthony T. Bogetti, Carla Calvó‐Tusell, Mac Kevin E. Braza, Lorenzo Casalino, Amanda J. Gramm, Sean M. Braet, Mia A. Rosenfeld, Harinda Rajapaksha, Bryan Barker, Ganesh S. Anand, Lillian T. Chong, Surl-Hee Ahn, Rommie E. Amaro
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.
Proceedings of the National Academy of Sciences · May 8, 2026Peer-reviewedBiophysics