The p53 gene acts as a tumor suppressor by inducing growth arrest or apoptosis during the cell cycle. Mutations of p53 are responsible for about half of all human cancers. Extensive research has been done on p53 and, more specifically, the protein’s DNA binding domain. Humans have nine splice-variant isoforms of p53: the full-length wildtype, and eight splice variants that contain truncated portions of the n-terminal and c-terminal. Most existing studies focus exclusively on the wildtype and its DNA binding domain, often excluding the n-terminal and c-terminal residues of the wildtype and these eight other isoforms altogether. My research serves to explore the behavior of the full-length wildtype p53 and its isoforms to learn about their potential regulatory effects using molecular dynamics simulations to determine the isoforms’ crystal structures.

Molecular dynamics simulations of the isoforms of p53

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.