Presenter: Ruben Sanchez – Biochemistry, Biology
Faculty Mentor(s): Marina Guenza
Session: (In-Person) Poster Presentation
Severe acute respiratory syndrome coronavirus 2 (SARS-Cov-2) utilizes a spike protein to recognize the receptor protein Angiotensin-converting enzyme 2 (ACE2) of human cells to initiate COVID-19. It is known that the spike protein adopts an active (open) conformation from an inactive (closed) conformation to initiate its infectious cycle. But it is unknown whether the different variants have mutations that affect the protein dynamics of the spike protein. It was hypothesized that the amino acid mutations of more transmissible variants will have increased protein dynamics leading to a dramatized Monod-Wyman-Changeux model. Identifying and targeting these dynamics may lead to the development of pharmaceuticals that may inhibit the infectivity of the SARS-CoV-2 virus. Therefore, two variants of the spike protein were analyzed using molecular dynamic simulations and the Langevin Equation for Protein Dynamics (LE4PD) to quantitively analyze residue fluctuation within their respective spike proteins. LE4PD quantified the protein dynamics and demonstrated that the more infectious variants have higher fluctuations in their protein dynamics.