The SARS-CoV-2 Spike variant D614G favors an open conformational state

• DOI: 10.1126/sciadv.abf3671
• Publication Date: 2021-04-16T19:26:57Z
• Authors: Rachael A. Mansbach; Srirupa Chakraborty; Kien Nguyen; David C. Montefiori; Bette Korber; S. Gnanakaran
• Keywords: 0301 basic medicine; 0303 health sciences; Glycosylation; SARS-CoV-2; Biophysics; COVID-19; Hydrogen Bonding; Molecular Dynamics Simulation; Virus Internalization; Antibodies, Neutralizing; Article; 3. Good health; Protein Subunits; 03 medical and health sciences; Mutation; Spike Glycoprotein, Coronavirus; Humans; Amino Acid Sequence; Angiotensin-Converting Enzyme 2; Protein Structure, Quaternary; Research Articles; Protein Binding

Symmetrization of contacts in D614G SARS-CoV-2 Spike favors greater probability of infection-capable conformation.