Borna Novak
Program: Computational and Systems Biology
Current advisor: Alex Holehouse, PhD
Undergraduate university: University of Sciences-Philadelphia
Research summary
A large fraction of proteins from the human proteome are classified as Intrinsically Disordered Proteins (IDPs). These proteins exhibit significant variability in their conformational states, lacking a stable, predefined three-dimensional structure. Instead, they undergo rapid transitions among a diverse set of configurations. Understanding the relationship between IDP’s sequences and their ensemble of conformations is crucial for deciphering their biological function. To gain insights into this relationship, I am employing a combination of computer simulations and bioinformatics. This interdisciplinary approach aims to uncover how the sequence of an IDP influences its conformational ensemble, ultimately shedding light on its functional properties.
Graduate publications
Chung, M. K. J.; Miller, R. J.; Novak, B.; Wang, Z.; Ponder, J. W. Accurate Host-Guest Binding Free Energies Using the AMOEBA Polarizable Force Field. J. Chem. Inf. Model. 2023, 63 (9), 2769–2782.