Dynamics of SARS-CoV-2 spike protein in open and closed states and identification of key structural perturbations upon mutations

<p>The SARS-Cov-2 spike protein resides on the exterior surface of the coronavirus, and therefore, acts as the first point of contact that mediates cell attachment and fusion. &nbsp;During this process, it undergoes dramatic conformational changes upon host receptor binding. We are leveraging high-performance computing to identify these structural perturbations in wildtype and mutant spike protein models. The files contain structures from molecular dynamics simulations of closed SARS-Cov-2 spike protein embedded in POPC membrane.</p>